Cited by 916Probiotics and Fermented FoodsBacterial Genetics and BiotechnologyMicrobial Inactivation Methods

The DOI matches its Crossref record; 647 of the 647 references it cites were found in a registry or an index.

Stress Physiology of Lactic Acid Bacteria.

Open access

Papadimitriou, Konstantinos, Alegría, Ángel, Bron, Peter A., de Angelis, Maria, Gobbetti, Marco, Kleerebezem, Michiel, Lemos, José A., Linares, Daniel M., Ross, Paul, Stanton, Catherine, Turroni, Francesca, van Sinderen, Douwe, Varmanen, Pekka, Ventura, Marco, Zúñiga, Manuel, Tsakalidou, Effie, Kok, Jan·2016·Microbiology and Molecular Biology Reviews

DOI 10.1128/mmbr.00076-15PMC PMC4981675

Open this paper in CoChat — free account Open PDF

Abstract

Lactic acid bacteria (LAB) are important starter, commensal, or pathogenic microorganisms. The stress physiology of LAB has been studied in depth for over 2 decades, fueled mostly by the technological implications of LAB robustness in the food industry. Survival of probiotic LAB in the host and the potential relatedness of LAB virulence to their stress resilience have intensified interest in the field. Thus, a wealth of information concerning stress responses exists today for strains as diverse as starter (e.g., Lactococcus lactis), probiotic (e.g., several Lactobacillus spp.), and pathogenic (e.g., Enterococcus and Streptococcus spp.) LAB. Here we present the state of the art for LAB stress behavior. We describe the multitude of stresses that LAB are confronted with, and we present the experimental context used to study the stress responses of LAB, focusing on adaptation, habituation, and cross-protection as well as on self-induced multistress resistance in stationary phase, biofilms, and dormancy. We also consider stress responses at the population and single-cell levels. Subsequently, we concentrate on the stress defense mechanisms that have been reported to date, grouping them according to their direct participation in preserving cell energy, defending macromolecules, and protecting the cell envelope. Stress-induced responses of probiotic LAB and commensal/pathogenic LAB are highlighted separately due to the complexity of the peculiar multistress conditions to which these bacteria are subjected in their hosts. Induction of prophages under environmental stresses is then discussed. Finally, we present systems-based strategies to characterize the "stressome" of LAB and to engineer new food-related and probiotic LAB with improved stress tolerance.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1128/mmbr.00076-15

Cites

647 of 647 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Items 201–400 of 647

Contribution of Glutathione Peroxidase to the Virulence of Streptococcus pyogenes
Brenot, A., King, K. Y., Janowiak, B. E., Griffith, O. W., & Caparon, M. G. (2003) · Infection and Immunity · doi:10.1128/iai.72.1.408-413.2004 · Cited by 148
Combined cold, acid, ethanol shocks in Oenococcus oeni: Effects on membrane fluidity and cell viability
Chu‐Ky, S., Tourdot‐Maréchal, R., Maréchal, P., & Guzzo, J. (2005) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2005.09.015 · Cited by 147
A sensor for intracellular ionic strength
Biemans‐Oldehinkel, E., Mahmood, N. A. B. N., & Poolman, B. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603871103 · Cited by 145
CovS Inactivates CovR and Is Required for Growth under Conditions of General Stress in Streptococcus pyogenes
Dalton, T. L., & Scott, J. R. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.12.3928-3937.2004 · Cited by 145
ClpP participates in the degradation of misfolded protein in Lactococcus lactis
Frees, D., & Ingmer, H. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01149.x · Cited by 144
Regulation and Physiologic Significance of the Agmatine Deiminase System of Streptococcus mutans UA159
Griswold, A. R., Jameson‐Lee, M., & Burne, R. A. (2006) · Journal of Bacteriology · doi:10.1128/jb.188.3.834-841.2006 · Cited by 143
CodY ofStreptococcus pneumoniae: Link between Nutritional Gene Regulation and Colonization
Hendriksen, W. T., Bootsma, H. J., Estevão, S., Hoogenboezem, T., de Jong, A., de Groot, R., Kuipers, O. P., & Hermans, P. W. M. (2007) · Journal of Bacteriology · doi:10.1128/jb.00917-07 · Cited by 143
Antimicrobial Peptide Resistance Mechanisms of Gram-Positive Bacteria
Nawrocki, K. L., Crispell, E., & McBride, S. M. (2014) · Antibiotics · doi:10.3390/antibiotics3040461 · Cited by 142
Overall control of nitrogen metabolism in Lactococcus lactis by CodY, and possible models for CodY regulation in Firmicutes
Guédon, É., Sperandio, B., Pons, N., Ehrlich, S. D., & Renault, P. (2005) · Microbiology · doi:10.1099/mic.0.28186-0 · Cited by 142
The PerR regulon in peroxide resistance and virulence of Streptococcus pyogenes
Brenot, A., King, K. Y., & Caparon, M. G. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04370.x · Cited by 141
Origin and analysis of microbial population heterogeneity in bioprocesses
Müller, S., Harms, H., & Bley, T. (2010) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2010.01.002 · Cited by 141
The LiaFSR System Regulates the Cell Envelope Stress Response inStreptococcus mutans
Suntharalingam, P., Senadheera, M. D., Mair, R. W., Levesque, C. M., & Cvitkovitch, D. G. (2009) · Journal of Bacteriology · doi:10.1128/jb.01563-08 · Cited by 141
Three gene products govern (p)ppGpp production by Streptococcus mutans
Lemos, J. A. C., Lin, V. K., Nascimento, M. M., Abranches, J., & Burne, R. A. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.05897.x · Cited by 140
Self-citation
Penicillin‐Binding Protein‐Mediated Resistance in Pneumococci and Staphylococci
Chambers, H. F. “. (1999) · The Journal of Infectious Diseases · doi:10.1086/513854 · Cited by 140
Leuconostoc gelidum sp. nov. and Leuconostoc carnosum sp. nov. from Chill-Stored Meats
Shaw, B., & Harding, C. D. (1989) · International Journal of Systematic Bacteriology · doi:10.1099/00207713-39-3-217 · Cited by 139
The fabM Gene Product of Streptococcus mutans Is Responsible for the Synthesis of Monounsaturated Fatty Acids and Is Necessary for Survival at Low pH
Fozo, E. M., & Quivey, R. G. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.13.4152-4158.2004 · Cited by 139
Molecular analysis of the psa permease complex of Streptococcus pneumoniae
McAllister, L. J., Tseng, H., Ogunniyi, A. D., Jennings, M. P., McEwan, A. G., & Paton, J. C. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04164.x · Cited by 138
Proteome analysis of Streptococcus mutans metabolic phenotype during acid tolerance
Len, A. C. L., Harty, D. W. S., & Jacques, N. A. (2004) · Microbiology · doi:10.1099/mic.0.26888-0 · Cited by 138
Microarray-Based Identification of htrA , a Streptococcus pneumoniae Gene That Is Regulated by the CiaRH Two-Component System and Contributes to Nasopharyngeal Colonization
Sebert, M., Palmer, L. M., Rosenberg, M., & Weiser, J. N. (2002) · Infection and Immunity · doi:10.1128/iai.70.8.4059-4067.2002 · Cited by 138
Postgenomic Analysis of Streptococcus thermophilus Cocultivated in Milk with Lactobacillus delbrueckii subsp. bulgaricus : Involvement of Nitrogen, Purine, and Iron Metabolism
Herve‐Jimenez, L., Guillouard, I., Guédon, É., Boudebbouze, S., Pascal Hols, A., Monnet, V., Maguin, E., & Rul, F. (2008) · Applied and Environmental Microbiology · doi:10.1128/aem.01984-08 · Cited by 136
Effect of Heat Shock or Cold Shock Treatment on the Resistance of Lactococcus lactis to Freezing and Lyophilization
Broadbent, J. R., & Lin, C. (1999) · Cryobiology · doi:10.1006/cryo.1999.2190 · Cited by 136
The ATP/Substrate Stoichiometry of the ATP-binding Cassette (ABC) Transporter OpuA
Patzlaff, J. S., van der Heide, T., & Poolman, B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304796200 · Cited by 134
Extracellular Zinc Competitively Inhibits Manganese Uptake and Compromises Oxidative Stress Management in Streptococcus pneumoniae
Eijkelkamp, B. A., Morey, J. R., Ween, M. P., Ong, C. Y., McEwan, A. G., Paton, J. C., & McDevitt, C. A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0089427 · Cited by 134
Cell wall modifications during osmotic stress in Lactobacillus casei
Piuri, M., Sánchez-Rivas, C., & Ruzal, S. M. (2004) · Journal of Applied Microbiology · doi:10.1111/j.1365-2672.2004.02428.x · Cited by 133
Regulation and Physiological Significance of ClpC and ClpP in Streptococcus mutans
Lemos, J. A. C., & Burne, R. A. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.22.6357-6366.2002 · Cited by 133
Self-citation
Structural and Functional Analysis of the Gene Cluster Encoding the Enzymes of the Arginine Deiminase Pathway of Lactobacillus sake
Zúñiga, M., Champomier-Vergès, M. C., Zagorec, M., & Pérez‐Martínez, G. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.16.4154-4159.1998 · Cited by 130
Self-citation
A camel passes through the eye of a needle: protein unfolding activity of Clp ATPases
Žółkiewski, M. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05309.x · Cited by 129
Regulation of Virulence by a Two-Component System in Group B Streptococcus
Jiang, S.-M., Cieslewicz, M. J., Kasper, D. L., & Wessels, M. R. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.3.1105-1113.2005 · Cited by 129
Vancomycin Resistance VanS/VanR Two-Component Systems
Hong, H., Hutchings, M. I., & Buttner, M. J. (2008) · Advances in experimental medicine and biology · doi:10.1007/978-0-387-78885-2_14 · Cited by 129
The novel transcriptional regulator SczA mediates protection against Zn2+stress by activation of the Zn2+‐resistance geneczcDinStreptococcus pneumoniae
Kloosterman, T. G., van der Kooi‐Pol, M. M., Bijlsma, J. J. E., & Kuipers, O. P. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.05849.x · Cited by 128
Pneumococcal histidine triad proteins are regulated by the Zn 2+ ‐dependent repressor AdcR and inhibit complement deposition through the recruitment of complement factor H
Ogunniyi, A. D., Grabowicz, M., Mahdi, L. K., Cook, J., Gordon, D. L., Sadlon, T. A., & Paton, J. C. (2009) · The FASEB Journal · doi:10.1096/fj.08-119537 · Cited by 127
Enterococcus faecalis Heme-Dependent Catalase
Frankenberg, L., Brugna, M., & Hederstedt, L. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.22.6351-6356.2002 · Cited by 127 · cited 1×
“up from the environment (259); its implication for virulence has”
Background
Lactic acid bacteria in dairy food: Surface characterization and interactions with food matrix components
Burgain, J., Scher, J., Francius, G., Borges, F., Corgneau, M., Revol‐Junelles, A., Cailliez‐Grimal, C., & Gaïani, C. (2014) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2014.09.005 · Cited by 127
Lipid II: A central component in bacterial cell wall synthesis and a target for antibiotics
KRUIJFF, B. D., van Dam, V., & Breukink, E. J. (2008) · Prostaglandins Leukotrienes and Essential Fatty Acids · doi:10.1016/j.plefa.2008.09.020 · Cited by 127
Heterologous Expression of BetL, a Betaine Uptake System, Enhances the Stress Tolerance ofLactobacillus salivariusUCC118
Sheehan, V. M., Sleator, R. D., Fitzgerald, G. F., & Hill, C. (2006) · Applied and Environmental Microbiology · doi:10.1128/aem.72.3.2170-2177.2006 · Cited by 127
Recent developments in copper and zinc homeostasis in bacterial pathogens
Braymer, J. J., & Giedroc, D. P. (2014) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2013.12.021 · Cited by 126
Basal Levels of (p)ppGpp in Enterococcus faecalis: the Magic beyond the Stringent Response
Gaca, A. O., Kajfasz, J. K., Miller, J. H., Liu, K., Wang, J. D., Abranches, J., & Lemos, J. A. C. (2013) · mBio · doi:10.1128/mbio.00646-13 · Cited by 126
Self-citation
Identification of Lactobacillus reuteri Genes Specifically Induced in the Mouse Gastrointestinal Tract
Walter, J., Heng, N. C. K., Hammes, W. P., Loach, D. M., Tannock, G. W., & Hertel, C. (2003) · Applied and Environmental Microbiology · doi:10.1128/aem.69.4.2044-2051.2003 · Cited by 126
Transport capabilities of eleven gram-positive bacteria: Comparative genomic analyses
Lorca, G. L., Barabote, R. D., Zlotopolski, V., Tran, C. V., Winnen, B., Hvorup, R. N., Stonestrom, A. J., Nguyen, E., Huang, L.-W., Kim, D. S., et al. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.02.007 · Cited by 125
Role of osmolytes in adaptation of osmotically stressed and chill-stressed Listeria monocytogenes grown in liquid media and on processed meat surfaces
Smith, L. T. (1996) · Applied and Environmental Microbiology · doi:10.1128/aem.62.9.3088-3093.1996 · Cited by 124
Trigger Factor inStreptococcus mutansIs Involved in Stress Tolerance, Competence Development, and Biofilm Formation
Wen, Z. T., Suntharaligham, P., Cvitkovitch, D. G., & Burne, R. A. (2004) · Infection and Immunity · doi:10.1128/iai.73.1.219-225.2005 · Cited by 124
Role of HtrA in the Virulence and Competence of Streptococcus pneumoniae
Ibrahim, Y. M., Kerr, A. R., McCluskey, J., & Mitchell, T. J. (2004) · Infection and Immunity · doi:10.1128/iai.72.6.3584-3591.2004 · Cited by 123
Transcriptional analysis of the Streptococcus mutans hrcA, grpE and dnaK genes and regulation of expression in response to heat shock and environmental acidification
Jayaraman, G., Penders, J. E. C., & Burne, R. A. (1997) · Molecular Microbiology · doi:10.1046/j.1365-2958.1997.4671835.x · Cited by 122
Intracellular pH is a major factor in the induction of tolerance to acid and other stresses in Lactococcus lactis
O’Sullivan, E. M., & Condon, S. (1997) · Applied and Environmental Microbiology · doi:10.1128/aem.63.11.4210-4215.1997 · Cited by 122
Quantitative Physiology of Saccharomyces cerevisiae at Near-Zero Specific Growth Rates
Boender, L. G. M., de Hulster, E. A. F., van Maris, A. J. A., Daran-Lapujade, P. A. S., & Pronk, J. T. (2009) · Applied and Environmental Microbiology · doi:10.1128/aem.00429-09 · Cited by 122
Oxidative stress in Lactococcus lactis.
Miyoshi, A., Rochat, T., Gratadoux, J., Loir, Y. L., Oliveira, S. C., Langella, P., & Azevedo, V. (2003) · PubMed · Cited by 122
Intersection of the stringent response and the CodY regulon in low GC Gram-positive bacteria
Geiger, T., & Wolz, C. (2013) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2013.11.013 · Cited by 121
Flow Cytometric Assessment of Membrane Integrity of Ethanol-StressedOenococcus oeniCells
Silveira, M. D. G. A., Romão, M. V. S., Loureiro-Dias, M. C., Rombouts, F. M., & Abee, T. (2002) · Applied and Environmental Microbiology · doi:10.1128/aem.68.12.6087-6093.2002 · Cited by 121
Glycine Betaine, Carnitine, and Choline Enhance Salinity Tolerance and Prevent the Accumulation of Sodium to a Level Inhibiting Growth of Tetragenococcus halophila
Robert, H., Marrec, C. L., Blanco, C., & Jebbar, M. (2000) · Applied and Environmental Microbiology · doi:10.1128/aem.66.2.509-517.2000 · Cited by 121
The role of transport processes in survival of lactic acid bacteria, Energy transduction and multidrug resistance
Konings, W. N., Lolkema, J. S., Bolhuis, H., van Veen, H. W., Poolman, B., & Driessen, A. J. M. (1997) · Antonie van Leeuwenhoek · doi:10.1023/a:1000143525601 · Cited by 120
Carbohydrate Starvation Causes a Metabolically Active but Nonculturable State in Lactococcus lactis
Ganesan, B., Stuart, M. R., & Weimer, B. C. (2007) · Applied and Environmental Microbiology · doi:10.1128/aem.01832-06 · Cited by 120
Super‐resolution microscopy reveals cell wall dynamics and peptidoglycan architecture in ovococcal bacteria
Wheeler, R., Mesnage, S., Boneca, I. G., Hobbs, J. K., & Foster, S. J. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07871.x · Cited by 120
Negative control in two-component signal transduction by transmitter phosphatase activity
Huynh, T. N., & Stewart, V. J. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07829.x · Cited by 119
The complete genomes of Lactobacillus plantarum and Lactobacillus johnsonii reveal extensive differences in chromosome organization and gene content.
Boekhorst, J., Siezen, R., Zwahlen, M., Vilanova, D., Pridmore, R., Mercenier, A., Kleerebezem, M., de Vos, W. D., Brüssow, H., & Desiere, F. (2004) · Microbiology · doi:10.1099/mic.0.27392-0 · Cited by 118
Self-citation
Glutamine, glutamate, and arginine-based acid resistance in Lactobacillus reuteri
Teixeira, J. S., Seeras, A., Sánchez-Maldonado, A. F., Zhang, C., Su, M. S., & Gänzle, M. G. (2014) · Food Microbiology · doi:10.1016/j.fm.2014.03.015 · Cited by 117
Analysis of Streptococcus mutans Proteins Modulated by Culture under Acidic Conditions
Wilkins, J. C., Homer, K. A., & Beighton, D. (2002) · Applied and Environmental Microbiology · doi:10.1128/aem.68.5.2382-2390.2002 · Cited by 117
Acquired Bacitracin Resistance in Enterococcus faecalis Is Mediated by an ABC Transporter and a Novel Regulatory Protein, BcrR
Manson, J. M., Keis, S., Smith, J. M. B., & Cook, G. M. (2004) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.48.10.3743-3748.2004 · Cited by 117
Functional implications of the microbial community structure of undefined mesophilic starter cultures
Smid, E. J., Erkus, O., Spus, M., Wolkers-Rooijackers, J. C., Alexeeva, S., & Kleerebezem, M. (2014) · Microbial Cell Factories · doi:10.1186/1475-2859-13-s1-s2 · Cited by 117
Self-citation
Transcriptome Analysis Reveals Mechanisms by Which Lactococcus lactis Acquires Nisin Resistance
Kramer, N. E., van Hijum, S. A. F. T., Knol, J., Kok, J., & Kuipers, O. P. (2006) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.50.5.1753-1761.2006 · Cited by 116
Self-citation
Effect of Heat Shock and Mutations in ClpL and ClpP on Virulence Gene Expression inStreptococcus pneumoniae
Kwon, H., Kim, S., Choi, M., Ogunniyi, A. D., Paton, J. C., Park, S.-H., Pyo, S., & Rhee, D. (2003) · Infection and Immunity · doi:10.1128/iai.71.7.3757-3765.2003 · Cited by 116
Stress Responses of Lactic Acid Bacteria
Tsakalidou, E., & Papadimitriou, K. (2011) · Springer eBooks · doi:10.1007/978-0-387-92771-8 · Cited by 116
Self-citation
Bioactives from probiotics for dermal health: functions and benefits
Lew, L.-C., & Liong, M.-T. (2013) · Journal of Applied Microbiology · doi:10.1111/jam.12137 · Cited by 115
Osmotic regulation of intracellular solute pools in Lactobacillus plantarum
Glaasker, E., Konings, W. N., & Poolman, B. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.3.575-582.1996 · Cited by 115
Two Spx Proteins Modulate Stress Tolerance, Survival, and Virulence in Streptococcus mutans
Kajfasz, J. K., Rivera-Ramos, I., Abranches, J., Martinez, A. R., Rosalen, P. L., Derr, A. M., Quivey, R. G., & Lemos, J. A. C. (2010) · Journal of Bacteriology · doi:10.1128/jb.00028-10 · Cited by 114
Self-citation
Lessons from 50 years of SOS DNA-damage-induced mutagenesis
Schlacher, K., & Goodman, M. F. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2198 · Cited by 114
Contribution of NADH Oxidase to Aerobic Metabolism of Streptococcus pyogenes
Gibson, C. M., Mallett, T. C., Claiborne, A., & Caparon, M. G. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.2.448-455.2000 · Cited by 114
The predicted secretome of Lactobacillus plantarum WCFS1 sheds light on interactions with its environment
Boekhorst, J., Wels, M., Kleerebezem, M., & Siezen, R. J. (2006) · Microbiology · doi:10.1099/mic.0.29217-0 · Cited by 114
Self-citation
Low pH-induced membrane fatty acid alterations in oral bacteria
Fozo, E. M., Kajfasz, J. K., & QUIVEYJR, R. (2004) · FEMS Microbiology Letters · doi:10.1016/j.femsle.2004.07.047 · Cited by 113
Respiration metabolism of Group B Streptococcus is activated by environmental haem and quinone and contributes to virulence
Yamamoto, Y., Poyart, C., Trieu‐Cuot, P., Lamberet, G., Gruss, A., & Gaudu, P. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04555.x · Cited by 113
uvrA Is an Acid-Inducible Gene Involved in the Adaptive Response to Low pH in Streptococcus mutans
Hanna, M. N., Ferguson, R. J., Li, Y.-H., & Cvitkovitch, D. G. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.20.5964-5973.2001 · Cited by 113
The quest for probiotic effector molecules—Unraveling strain specificity at the molecular level
Lee, I.-C., Tomita, S., Kleerebezem, M., & Bron, P. A. (2012) · Pharmacological Research · doi:10.1016/j.phrs.2012.09.010 · Cited by 112
Self-citation
Role of RegM, a Homologue of the Catabolite Repressor Protein CcpA, in the Virulence of Streptococcus pneumoniae
Giammarinaro, P., & Paton, J. C. (2002) · Infection and Immunity · doi:10.1128/iai.70.10.5454-5461.2002 · Cited by 112
Comparative analysis of the Oenococcus oeni pan genome reveals genetic diversity in industrially-relevant pathways
Borneman, A. R., McCarthy, J. M., Chambers, P. J., & Bartowsky, E. J. (2012) · BMC Genomics · doi:10.1186/1471-2164-13-373 · Cited by 112
Expression of the virulence‐related Sca (Mn2+) permease in Streptococcus gordonii is regulated by a diphtheria toxin metallorepressor‐like protein ScaR
Jakubovics, N. S., Smith, A. W., & Jenkinson, H. F. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.02122.x · Cited by 111
Interplay of heritage and habitat in the distribution of bacterial signal transduction systems
Galperin, M. Y., Higdon, R., & Kolker, E. (2010) · Molecular BioSystems · doi:10.1039/b908047c · Cited by 111
Augmented Production of Extracellular Superoxide by Blood Isolates of Enterococcus faecalis
Huycke, M. M., Joyce, W., & Wack, M. F. (1996) · The Journal of Infectious Diseases · doi:10.1093/infdis/173.3.743 · Cited by 110
Proteomic analysis of responses of a new probiotic bacterium Lactobacillus casei Zhang to low acid stress
Wu, R., Zhang, W., Sun, T., Wu, J., Yue, X., Meng, H., & Zhang, H. (2011) · International Journal of Food Microbiology · doi:10.1016/j.ijfoodmicro.2011.04.003 · Cited by 109
Lifestyle of Lactobacillus plantarum in the mouse caecum
Marco, M. L., Peters, T. H. F., Bongers, R. S., Douwe Molenaar, B., van Hemert, S., Sonnenburg, J. L., Gordon, J. I., & Kleerebezem, M. (2009) · Environmental Microbiology · doi:10.1111/j.1462-2920.2009.02001.x · Cited by 109
Self-citation
Eukaryotic-Type Serine/Threonine Protein Kinase StkP Is a Global Regulator of Gene Expression inStreptococcus pneumoniae
Sasková, L., Nováková, L., Basler, M., & Branny, P. (2007) · Journal of Bacteriology · doi:10.1128/jb.01616-06 · Cited by 109
Improved adaptation to heat, cold, and solvent tolerance in Lactobacillus plantarum
Fiocco, D., Capozzi, V., Goffin, P., Pascal Hols, A., & Spano, G. (2007) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-007-1228-x · Cited by 108
Novel inhibitors of bacterial cell wall synthesis
Silver, L. L. (2003) · Current Opinion in Microbiology · doi:10.1016/j.mib.2003.08.004 · Cited by 108
Involvement of Sensor Kinases in the Stress Tolerance Response ofStreptococcus mutans
Biswas, I., Drake, L., Erkina, D., & Biswas, S. (2007) · Journal of Bacteriology · doi:10.1128/jb.00990-07 · Cited by 107
Low pH-induced membrane fatty acid alterations in oral bacteria
Fozo, E. M., Kajfasz, J. K., & Quivey, R. G. (2004) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2004.tb09769.x · Cited by 107
Oxygen metabolism of Streptococcus mutans: uptake of oxygen and release of superoxide and hydrogen peroxide
Thomas, E. L., & Pera, K. (1983) · Journal of Bacteriology · doi:10.1128/jb.154.3.1236-1244.1983 · Cited by 106
Convergence in probiotic Lactobacillus gut-adaptive responses in humans and mice
Marco, M. L., de Vries, M. C., Wels, M., Douwe Molenaar, B., Mangell, P., Ahrné, S., de Vos, W. M., Vaughan, E. E., & Kleerebezem, M. (2010) · The ISME Journal · doi:10.1038/ismej.2010.61 · Cited by 105
Self-citation
Proteomic Profiling of the Acid Stress Response in Lactobacillus plantarum 423
Heunis, T. D. J., Deane, S. M., Smit, S., & Dicks, L. M. T. (2014) · Journal of Proteome Research · doi:10.1021/pr500353x · Cited by 105
Characteristics and osmoregulatory roles of uptake systems for proline and glycine betaine in Lactococcus lactis
Douwe Molenaar, B., Hagting, A., Alkema, H. J., Driessen, A. J. M., & Konings, W. N. (1993) · Journal of Bacteriology · doi:10.1128/jb.175.17.5438-5444.1993 · Cited by 104
Transcriptional Regulation of the Streptococcus salivarius 57.I Urease Operon
Chen, Y. M., Weaver, C. A., Mendelsohn, D. R., & Burne, R. A. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.21.5769-5775.1998 · Cited by 104
BcrC from Bacillus subtilis Acts as an Undecaprenyl Pyrophosphate Phosphatase in Bacitracin Resistance
Bernard, R., Ghachi, M. E., Mengin‐Lecreulx, D., Chippaux, M., & Denizot, F. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413750200 · Cited by 104
Formation of Hydrogen Peroxide by Group N Streptococci and Its Effect on Their Growth and Metabolism
Anders, R. F., Hogg, D. M., & Jago, G. R. (1970) · Applied Microbiology · doi:10.1128/am.19.4.608-612.1970 · Cited by 104
DNA Macroarray Profiling of Lactococcus lactis subsp. lactis IL1403 Gene Expression during Environmental Stresses
Xie, Y., Chou, L., Cutler, A., & Weimer, B. C. (2004) · Applied and Environmental Microbiology · doi:10.1128/aem.70.11.6738-6747.2004 · Cited by 104
Exchange of Aspartate and Alanine
Abe, K., Hayashi, H., & Maloney, P. C. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.6.3079 · Cited by 103
Characterization and Functional Analysis of the poxB Gene, Which Encodes Pyruvate Oxidase in Lactobacillus plantarum
Lorquet, F., Goffin, P., Muscariello, L., Baudry, J.-B., Ladero, V., Sacco, M., Kleerebezem, M., & Pascal Hols, A. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.12.3749-3759.2004 · Cited by 103
Self-citation
Impact of Aeration and Heme-Activated Respiration on Lactococcus lactis Gene Expression: Identification of a Heme-Responsive Operon
Pedersen, M. B., Garrigues, C., Tuphile, K., Brun, C., Vido, K., Bennedsen, M., Møllgaard, H., Gaudu, P., & Gruss, A. (2008) · Journal of Bacteriology · doi:10.1128/jb.00447-08 · Cited by 103
Role of Methionine Sulfoxide Reductases A and B of Enterococcus faecalis in Oxidative Stress and Virulence
Chen, Z., Hartke, A., Sorda, M. L., Posteraro, B., Laplace, J., Auffray, Y., & Sanguinetti, M. (2010) · Infection and Immunity · doi:10.1128/iai.00165-10 · Cited by 103
Differential gene expression in response to phenol and catechol reveals different metabolic activities for the degradation of aromatic compounds in Bacillus subtilis
Tam, L. T., Eymann, C., Albrecht, D., Sietmann, R., Schauer, F., Hecker, M., & Antelmann, H. (2006) · Environmental Microbiology · doi:10.1111/j.1462-2920.2006.01034.x · Cited by 102
Role of the dpr Product in Oxygen Tolerance in Streptococcus mutans
Yamamoto, Y., Higuchi, M., Poole, L. B., & Kamio, Y. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.13.3740-3747.2000 · Cited by 102
Role for Serine Protease HtrA (DegP) ofStreptococcus pyogenesin the Biogenesis of Virulence Factors SpeB and the Hemolysin Streptolysin S
Lyon, W. R., & Caparon, M. G. (2004) · Infection and Immunity · doi:10.1128/iai.72.3.1618-1625.2004 · Cited by 102
ThesloABCROperon ofStreptococcus mutansEncodes an Mn and Fe Transport System Required for Endocarditis Virulence and Its Mn-Dependent Repressor
Paik, S., Brown, A., Munro, C. L., Cornelissen, C. N., & Kitten, T. O. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.20.5967-5975.2003 · Cited by 102
Decreased necrotizing fasciitis capacity caused by a single nucleotide mutation that alters a multiple gene virulence axis
Olsen, R. J., Sitkiewicz, I., Ayeras, A. A., Gonulal, V. E., Cantu, C. C., Beres, S. B., Green, N. M., Lei, B., Humbird, T. L., Greaver, J. L., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911811107 · Cited by 101
SpxB Regulates O-Acetylation-dependent Resistance of Lactococcus lactis Peptidoglycan to Hydrolysis
Veiga, P., Bulbarela-Sampieri, C., Furlan, S., Maisons, A., Chapot, M.-P., Erkelenz, M., Mervelet, P., Noirot, P. H., Frees, D., Kuipers, O. P., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611308200 · Cited by 101
Self-citation
Cell envelope stress induced by the bacteriocin Lcn972 is sensed by the lactococcal two‐component system CesSR
Martı́nez, B., Zomer, A., Rodrı́guez, A., Kok, J., & Kuipers, O. P. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.05668.x · Cited by 101
Self-citation
Acid adaptation ofLactobacillus delbrueckiisubsp.bulgaricusinduces physiological responses at membrane and cytosolic levels that improves cryotolerance
Streit, F., Delettre, J., Corrieu, G., & Béal, C. (2008) · Journal of Applied Microbiology · doi:10.1111/j.1365-2672.2008.03848.x · Cited by 100
Rgg Coordinates Virulence Factor Synthesis and Metabolism inStreptococcus pyogenes
Chaussee, M. S., Somerville, G. A., Reitzer, L., & Musser, J. M. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.20.6016-6024.2003 · Cited by 100
Enterococcus faecalis V583 Contains a Cytochrome bd -Type Respiratory Oxidase
Winstedt, L., Frankenberg, L., Hederstedt, L., & von Wachenfeldt, C. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.13.3863-3866.2000 · Cited by 99
Genetic and Biochemical Characterization of a High-Affinity Betaine Uptake System (BusA) in Lactococcus lactis Reveals a New Functional Organization within Bacterial ABC Transporters
Obis, D., Guillot, A., Gripon, J. C., Renault, P., Bolotin, A., & Mistou, M. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.20.6238-6246.1999 · Cited by 99
Functional Analysis of Three Plasmids from Lactobacillus plantarum
van Kranenburg, R., Golić, N., Bongers, R. S., Leer, R. J., de Vos, W. M., Siezen, R. J., & Kleerebezem, M. (2005) · Applied and Environmental Microbiology · doi:10.1128/aem.71.3.1223-1230.2005 · Cited by 98
Self-citation
Physiologic Effects of Forced Down-Regulation of dnaK and groEL Expression in Streptococcus mutans
Lemos, J. A. C., Luzardo, Y., & Burne, R. A. (2006) · Journal of Bacteriology · doi:10.1128/jb.01655-06 · Cited by 98
Self-citation
Regulation of Iron Transport inStreptococcus pneumoniaeby RitR, an Orphan Response Regulator
Ulijasz, A. T., Andes, D. R., Glasner, J. D., & Weisblum, B. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.23.8123-8136.2004 · Cited by 97
Import and Metabolism of Glutathione by Streptococcus mutans
Sherrill, C. B., & Fahey, R. C. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.6.1454-1459.1998 · Cited by 97
Control of Virulence by the Two-Component System CiaR/H Is Mediated via HtrA, a Major Virulence Factor ofStreptococcus pneumoniae
Ibrahim, Y. M., Kerr, A. R., McCluskey, J., & Mitchell, T. J. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.16.5258-5266.2004 · Cited by 97
A small heat shock protein from Leuconostoc oenos induced by multiple stresses and during stationary growth phase
Guzzo, J., Delmas, F., Pierre, F., Jobin, M.-P., Samyn, B., BEEUMEN, J. V., Cavin, J., & Diviès, C. (1997) · Letters in Applied Microbiology · doi:10.1046/j.1472-765x.1997.00042.x · Cited by 96
Small regulatory RNAs from low-GC Gram-positive bacteria
Brantl, S., & Brückner, R. (2014) · RNA Biology · doi:10.4161/rna.28036 · Cited by 96
Role of Clp Proteins in Expression of Virulence Properties ofStreptococcus mutans
Kajfasz, J. K., Martinez, A. R., Rivera-Ramos, I., Abranches, J., Koo, H., Quivey, R. G., & Lemos, J. A. C. (2009) · Journal of Bacteriology · doi:10.1128/jb.01609-08 · Cited by 96
Self-citation
Evolution of Transmembrane Protein Kinases Implicated in Coordinating Remodeling of Gram-Positive Peptidoglycan: Inside versus Outside
Jones, G., & Dyson, P. (2006) · Journal of Bacteriology · doi:10.1128/jb.00800-06 · Cited by 96
Antimicrobial agents targeting bacterial cell walls and cell membranes
Bush, K. (2012) · Scientific and Technical Review (World Organisation for Animal Health) · doi:10.20506/rst.31.1.2096 · Cited by 96
A PerR‐regulated metal transporter (PmtA) is an interface between oxidative stress and metal homeostasis in Streptococcus pyogenes
Brenot, A., Weston, B. F., & Caparon, M. G. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05577.x · Cited by 95
The Role of Cold-Shock Proteins in Low-Temperature Adaptation of Food-Related Bacteria
Wouters, J. A., ROMBOUTS, F. M., Kuipers, O. P., de Vos, W. M., & Abee, T. (2000) · Systematic and Applied Microbiology · doi:10.1016/s0723-2020(00)80001-6 · Cited by 95
The Regulator PerR Is Involved in Oxidative Stress Response and Iron Homeostasis and Is Necessary for Full Virulence of Streptococcus pyogenes
Ricci, S., Janulczyk, R., & Björck, L. (2002) · Infection and Immunity · doi:10.1128/iai.70.9.4968-4976.2002 · Cited by 95
Analysis of an Agmatine Deiminase Gene Cluster in Streptococcus mutans UA159
Griswold, A. R., Chen, Y. M., & Burne, R. A. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.6.1902-1904.2004 · Cited by 95
Rerouting of pyruvate metabolism during acid adaptation in Lactobacillus bulgaricus
Fernandez, A., Ogawa, J., Penaud, S., Boudebbouze, S., Ehrlich, S. D., van de Guchte, M., & Maguin, E. (2008) · PROTEOMICS · doi:10.1002/pmic.200700974 · Cited by 94
CtsR, the Gram‐positive master regulator of protein quality control, feels the heat
Elsholz, A. K. W., Michalik, S., Zühlke, D., Hecker, M., & Gerth, U. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.228 · Cited by 94
Analysis of the Transcriptome of Group A Streptococcus in Mouse Soft Tissue Infection
Graham, M., Virtaneva, K. I., Porcella, S. F., Gardner, D. J., Long, R. D., Welty, D. M., Barry, W. T., Johnson, C. A., Parkins, L. D., Wright, F. A., et al. (2006) · American Journal Of Pathology · doi:10.2353/ajpath.2006.060112 · Cited by 94
A liaR Deletion Restores Susceptibility to Daptomycin and Antimicrobial Peptides in Multidrug-Resistant Enterococcus faecalis
Reyes, J., Panesso, D., Tran, T. T., Mishra, N. N., Cruz, M. R., Munita, J. M., Singh, K. V., Yeaman, M. R., Murray, B. E., Shamoo, Y., et al. (2015) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiu602 · Cited by 94
Effects of metabolic flux on stress response pathways in Lactococcus lactis
Duwat, P., Ehrlich, S. D., & Gruss, A. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01222.x · Cited by 94
CcpA regulation of aerobic and respiration growth in Lactococcus lactis
Gaudu, P., Lamberet, G., Poncet, S., & Gruss, A. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03700.x · Cited by 94
A new structural paradigm in copper resistance in Streptococcus pneumoniae
Fu, Y., Tsui, H.-C. T., Bruce, K. E., Sham, L.-T., Higgins, K. A., Lisher, J. P., Kazmierczak, K. M., Maroney, M. J., Dann, C. E., Winkler, M. E., et al. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1168 · Cited by 93
Role of Transporter Proteins in Bile Tolerance ofLactobacillus acidophilus
Pfeiler, E. A., & Klaenhammer, T. R. (2009) · Applied and Environmental Microbiology · doi:10.1128/aem.00495-09 · Cited by 92
The Metalloregulatory Zinc Site in Streptococcus pneumoniae AdcR, a Zinc-activated MarR Family Repressor
Reyes-Caballero, H., Guerra, A. J., Jacobsen, F. E., Kazmierczak, K. M., Cowart, D. M., Koppolu, U. M. K., Scott, R. A., Winkler, M. E., & Giedroc, D. P. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.08.030 · Cited by 92
Proteins of rat serum, urine, and cerebrospinal fluid: VI. Further protein identifications and interstrain comparison
Wait, R., Gianazza, E., Eberini, I., Sironi, L., Dunn, M. J., Gemeiner, M., & Miller, I. (2001) · Electrophoresis · doi:10.1002/1522-2683(200108)22:14 · Cited by 91
Regulation of stress response in Oenococcus oeni as a function of environmental changes and growth phase
Guzzo, J., Jobin, M.-P., Delmas, F., Fortier, L., Garmyn, D., Tourdot‐Maréchal, R., Lee, B. H., & Diviès, C. (2000) · International Journal of Food Microbiology · doi:10.1016/s0168-1605(00)00209-9 · Cited by 91
Fermentation and proteome profiles of Lactobacillus plantarum strains during growth under food-like conditions
Siragusa, S., Angelis, M. D., Calasso, M. P., Campanella, D., Minervini, F., Cagno, R. D., & Gobbetti, M. (2013) · Journal of Proteomics · doi:10.1016/j.jprot.2013.11.003 · Cited by 91
Self-citation
LAB-Secretome: a genome-scale comparative analysis of the predicted extracellular and surface-associated proteins of Lactic Acid Bacteria
Zhou, M., Theunissen, D. H. J., Wels, M., & Siezen, R. J. (2010) · BMC Genomics · doi:10.1186/1471-2164-11-651 · Cited by 90
Dynamic response of catabolic pathways to autoacidification in Lactococcus lactis: transcript profiling and stability in relation to metabolic and energetic constraints
Even, S., Lindley, N. D., Loubière, P., & Cocaign‐Bousquet, M. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.03086.x · Cited by 90
Transcriptome analysis of the secretion stress response of Bacillus subtilis
Hyyryläinen, H., Sarvas, M., & Kontinen, V. P. (2005) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-005-1898-1 · Cited by 89
Maintaining network security: how macromolecular structures cross the peptidoglycan layer
Scheurwater, E. M., & Burrows, L. L. (2011) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2011.02228.x · Cited by 88
AsrR Is an Oxidative Stress Sensing Regulator Modulating Enterococcus faecium Opportunistic Traits, Antimicrobial Resistance, and Pathogenicity
Lebreton, F., van Schaik, W., Sanguinetti, M., Posteraro, B., Torelli, R., Bras, F. L., Verneuil, N., Zhang, X., Giárd, J.-C., Dhalluin, A., et al. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002834 · Cited by 88
Defects in ex vivo and in vivo growth and sensitivity to osmotic stress of group A Streptococcus caused by interruption of response regulator gene vicR
Liu, M., Hanks, T. S., Zhang, J., McClure, M. J., Siemsen, D. W., Elser, J. L., Quinn, M. T., & Lei, B. (2006) · Microbiology · doi:10.1099/mic.0.28706-0 · Cited by 88
Proteomic and transcriptomic analysis of the response to bile stress of Lactobacillus casei BL23
Alcántara, C., & Zúñiga, M. (2012) · Microbiology · doi:10.1099/mic.0.055657-0 · Cited by 87
Self-citation
Cell surface-associated compounds of probiotic lactobacilli sustain the strain-specificity dogma
Bron, P. A., Tomita, S., Mercenier, A., & Kleerebezem, M. (2013) · Current Opinion in Microbiology · doi:10.1016/j.mib.2013.06.001 · Cited by 86
Self-citation
CsrRS Regulates Group BStreptococcusVirulence Gene Expression in Response to Environmental pH: a New Perspective on Vaccine Development
Santi, I., Grifantini, R., Jiang, S.-M., Brettoni, C., Grandi, G., Wessels, M. R., & Soriani, M. (2009) · Journal of Bacteriology · doi:10.1128/jb.00370-09 · Cited by 86
Oxygen utilization by Lactobacillus plantarum
G�tz, F., Sedewitz, B., & Elstner, E. F. (1980) · Archives of Microbiology · doi:10.1007/bf00446878 · Cited by 85
Proteome Analyses of Heme-Dependent Respiration inLactococcus lactis: Involvement of the Proteolytic System
Vido, K., Bars, D. L., Mistou, M., Anglade, P., Gruss, A., & Gaudu, P. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.6.1648-1657.2004 · Cited by 85
Accumulation of Polyphosphate in Lactobacillus spp. and Its Involvement in Stress Resistance
Alcántara, C., Blasco, A., Zúñiga, M., & Monedero, V. (2013) · Applied and Environmental Microbiology · doi:10.1128/aem.03997-13 · Cited by 84
Self-citation
TheftsHGene of the Wine BacteriumOenococcus oeniIs Involved in Protection against Environmental Stress
Bourdineaud, J., Nehmé, B., Tesse, S., & Lonvaud‐Funel, A. (2003) · Applied and Environmental Microbiology · doi:10.1128/aem.69.5.2512-2520.2003 · Cited by 83
Evolutionary engineering to enhance starter culture performance in food fermentations
Bachmann, H., Pronk, J. T., Kleerebezem, M., & Teusink, B. (2014) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2014.09.003 · Cited by 83
Self-citation
Comparative proteome approach to characterize the high‐pressure stress response of Lactobacillus sanfranciscensis DSM 20451T
Hörmann, S., Scheyhing, C. H., Behr, J., Pavlovic, M., Ehrmann, M. A., & Vogel, R. F. (2006) · PROTEOMICS · doi:10.1002/pmic.200402086 · Cited by 83
Conserved DegP Protease in Gram-Positive Bacteria Is Essential for Thermal and Oxidative Tolerance and Full Virulence in Streptococcus pyogenes
Jones, C. H., Bolken, T. C., Jones, K. F., Zeller, G. O., & Hruby, D. E. (2001) · Infection and Immunity · doi:10.1128/iai.69.9.5538-5545.2001 · Cited by 83
The bacA gene, which determines bacitracin susceptibility in Streptococcus pneumoniae and Staphylococcus aureus, is also required for virulence The GenBank accession number for the sequence reported in this paper is AF228662.
Chalker, A. F., Ingraham, K. A., Lunsford, R. D., Bryant, A. P., Bryant, J., Wallis, N. G., Broskey, J. P., Pearson, S. C., & Holmes, D. J. (2000) · Microbiology · doi:10.1099/00221287-146-7-1547 · Cited by 83
The Streptococcus mutans Serine/Threonine Kinase, PknB, Regulates Competence Development, Bacteriocin Production, and Cell Wall Metabolism
Banu, L. D., Conrads, G., Rehrauer, H., Hussain, H. A., Allan, E., & van der Ploeg, J. R. (2010) · Infection and Immunity · doi:10.1128/iai.01167-09 · Cited by 83
Autoinducer-2 influences interactions amongst pioneer colonizing streptococci in oral biofilms
Cuadra-Saenz, G., Rao, D. L., Underwood, A. J., Belapure, S. A., Campagna, S. R., Sun, Z., Tammariello, S. P., & Rickard, A. H. (2012) · Microbiology · doi:10.1099/mic.0.057182-0 · Cited by 82
Generic and Specific Adaptive Responses ofStreptococcus pneumoniaeto Challenge with Three Distinct Antimicrobial Peptides, Bacitracin, LL-37, and Nisin
Majchrzykiewicz, J. A., Kuipers, O. P., & Bijlsma, J. J. E. (2009) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00769-09 · Cited by 82
Molecular and Functional Analyses of the metC Gene of Lactococcus lactis , Encoding Cystathionine β-Lyase
Fernández, M., van Doesburg, W., Rutten, G., Marugg, J. D., Alting, A. C., van Kranenburg, R., & Kuipers, O. P. (2000) · Applied and Environmental Microbiology · doi:10.1128/aem.66.1.42-48.2000 · Cited by 82
Cytotoxicity of Hydrogen Peroxide Produced by Enterococcus faecium
Moy, T. I., Mylonakis, E. E., Calderwood, S. B., & Ausubel, F. M. (2004) · Infection and Immunity · doi:10.1128/iai.72.8.4512-4520.2004 · Cited by 82
New insights in the molecular biology and physiology ofStreptococcus thermophilusrevealed by comparative genomics
Pascal Hols, A., Hancy, F., Fontaine, L., Grossiord, B., Prozzi, D., Leblond‐Bourget, N., Decaris, B., Bolotin, A., Delorme, C., Ehrlich, S. D., et al. (2005) · FEMS Microbiology Reviews · doi:10.1016/j.fmrre.2005.04.008 · Cited by 82
Self-citation
Identification of Multiple Substrates of the StkP Ser/Thr Protein Kinase in Streptococcus pneumoniae
Nováková, L., Bezoušková, S., Pompach, P., Spidlova, P., Sasková, L., Weiser, J., & Branny, P. (2010) · Journal of Bacteriology · doi:10.1128/jb.01564-09 · Cited by 81
Heat Resistance and Salt Hypersensitivity in Lactococcus lactis Due to Spontaneous Mutation of llmg_1816 ( gdpP ) Induced by High-Temperature Growth
Smith, W. M., Pham, H. T., Lei, L., Dou, J., Soomro, A. H., Beatson, S. A., Dykes, G. A., & Turner, M. S. (2012) · Applied and Environmental Microbiology · doi:10.1128/aem.02316-12 · Cited by 81
Adaptive Acid Tolerance Response of Streptococcus sobrinus
Nascimento, M. M., Lemos, J. A. C., Abranches, J., Gonçalves, R. B., & Burne, R. A. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.19.6383-6390.2004 · Cited by 81
Self-citation
The effect of low pH on protein expression by the probiotic bacterium Lactobacillus reuteri
Lee, K., Lee, H., Pi, K., & Choi, Y. (2008) · PROTEOMICS · doi:10.1002/pmic.200700663 · Cited by 80
Recognition of peptidoglycan and β-lactam antibiotics by the extracellular domain of the Ser/Thr protein kinase StkP fromStreptococcus pneumoniae
Maestro, B., Nováková, L., Hesek, D., Lee, M., Leyva‐Díaz, E., Mobashery, S., Sanz, J. M., & Branny, P. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.12.016 · Cited by 80
Roles of relSpn in stringent response, global regulation and virulence of serotype 2 Streptococcus pneumoniae D39
Kazmierczak, K. M., Wayne, K. J., Rechtsteiner, A., & Winkler, M. E. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06669.x · Cited by 80
Characterization of the CopR Regulon ofLactococcus lactisIL1403
Magnani, D., Barré, O., Gerber, S. D., & Solioz, M. (2007) · Journal of Bacteriology · doi:10.1128/jb.01481-07 · Cited by 79
Proton-Translocating Adenosine Triphosphatase Activity in Lactic Acid Bacterial
Nannen, N. L., & Hutkins, R. W. (1991) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(91)78220-9 · Cited by 79
Contribution of the ATP-Dependent Protease ClpCP to the Autolysis and Virulence of Streptococcus pneumoniae
Ibrahim, Y. M., Kerr, A. R., Silva, N. A., & Mitchell, T. J. (2005) · Infection and Immunity · doi:10.1128/iai.73.2.730-740.2005 · Cited by 78
Correlation of oxygen utilization and hydrogen peroxide accumulation with oxygen induced enzymes in Lactobacillus plantarum cultures
Murphy, M. G., & Condon, S. (1984) · Archives of Microbiology · doi:10.1007/bf00425405 · Cited by 78
The BceABRS Four-Component System Regulates the Bacitracin-Induced Cell Envelope Stress Response in Streptococcus mutans
Ouyang, J., Tian, X., Versey, J., Wishart, A., & Li, Y.-H. (2010) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01802-09 · Cited by 78
Importance ofgls24in Virulence and Stress Response ofEnterococcus faecalisand Use of the Gls24 Protein as a Possible Immunotherapy Target
Teng, F., Nannini, E. C., & Murray, B. E. (2005) · The Journal of Infectious Diseases · doi:10.1086/427191 · Cited by 78
Reciprocal Regulation of Cephalosporin Resistance in Enterococcus faecalis
Kristich, C. J., Little, J. L., Hall, C. L., & Hoff, J. S. (2011) · mBio · doi:10.1128/mbio.00199-11 · Cited by 78
Involvement of Pyruvate Oxidase Activity and Acetate Production in the Survival of Lactobacillus plantarum during the Stationary Phase of Aerobic Growth
Goffin, P., Muscariello, L., Lorquet, F., Stukkens, A., Prozzi, D., Sacco, M., Kleerebezem, M., & Pascal Hols, A. (2006) · Applied and Environmental Microbiology · doi:10.1128/aem.00659-06 · Cited by 78
Self-citation
CtsR Is the Master Regulator of Stress Response Gene Expression inOenococcus oeni
Grandvalet, C., Coucheney, F., Beltramo, C., & Guzzo, J. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.16.5614-5623.2005 · Cited by 78
The Enterococcus faecalis superoxide dismutase is essential for its tolerance to vancomycin and penicillin
Bizzini, A., Zhao, C., Auffray, Y., & Hartke, A. (2009) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkp369 · Cited by 78
Stress Responses in ProbioticLactobacillus casei
Hosseininezhad, M., Hussain, M. A., & Britz, M. L. (2013) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2012.675601 · Cited by 77
Improved Adaptation to Cold-Shock, Stationary-Phase, and Freezing Stresses in Lactobacillus plantarum Overproducing Cold-Shock Proteins
Derzelle, S., Hallet, B., Ferain, T., Delcour, J., & Pascal Hols, A. (2003) · Applied and Environmental Microbiology · doi:10.1128/aem.69.7.4285-4290.2003 · Cited by 77
Proteomic characterization of the acid tolerance response in L actobacillus delbrueckii subsp. bulgaricus CAUH1 and functional identification of a novel acid stress‐related transcriptional regulator L db0677
Zhai, Z., Douillard, F. P., An, H., Wang, G., Guo, X., Luo, Y., & Hao, Y. (2013) · Environmental Microbiology · doi:10.1111/1462-2920.12280 · Cited by 76
Auxiliary phosphatases in two-component signal transduction
Silversmith, R. E. (2010) · Current Opinion in Microbiology · doi:10.1016/j.mib.2010.01.004 · Cited by 76
Systemic inactivation and phenotypic characterization of two-component systems in expression of Streptococcus mutans virulence properties
Levesque, C. M., Mair, R. W., Perry, J. A., Lau, P. C. Y., Li, Y.-H., & Cvitkovitch, D. G. (2007) · Letters in Applied Microbiology · doi:10.1111/j.1472-765x.2007.02203.x · Cited by 76
Identification ofStreptococcus thermophilusCNRZ368 Genes Involved in Defense against Superoxide Stress
Thibessard, A., Borges, F., Fernandez, A., Gintz, B., Decaris, B., & Leblond‐Bourget, N. (2004) · Applied and Environmental Microbiology · doi:10.1128/aem.70.4.2220-2229.2004 · Cited by 76
Six putative two-component regulatory systems isolated from Lactococcus lactis subsp. cremoris MG1363 The GenBank accession numbers for the sequences of the six 2CSs and surrounding ORFs determined in this work are AF172649, AF176556, AF178425, AF172650, AF176557 and AF176809 for systems A–F, respectively.
Motherway, M. O., van Sinderen, D., MOREL‐DEVILLE, F., Fitzgerald, G. F., Ehrlich, S. D., & Morel, P. (2000) · Microbiology · doi:10.1099/00221287-146-4-935 · Cited by 76
P2CS: a database of prokaryotic two-component systems
Barakat, M., Ortet, P., & Whitworth, D. E. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq1023 · Cited by 76
Sequencing, characterization and transcriptional analysis of the histidine decarboxylase operon of Lactobacillus buchneri
Martín, M. C., Fernández, M., Linares, D. M., & Álvarez, M. A. (2005) · Microbiology · doi:10.1099/mic.0.27459-0 · Cited by 75
Self-citation
Understanding the physiology of Lactobacillus plantarum at zero growth
Goffin, P., van de Bunt, B., Giovane, M., Leveau, J. H. J., Höppener‐Ogawa, S., Teusink, B., & Hugenholtz, J. (2010) · Molecular Systems Biology · doi:10.1038/msb.2010.67 · Cited by 75
Induction of SOS functions by alkaline intracellular pH in Escherichia coli
Schuldiner, S., AGMON, V., Brandsma, J. A., Cohen, A., Friedman, E. D., & Padan, E. (1986) · Journal of Bacteriology · doi:10.1128/jb.168.2.936-939.1986 · Cited by 74
TheLactococcus lactisplasmidome: much learnt, yet still lots to discover
Ainsworth, S., Stockdale, S. R., Bottacini, F., Mahony, J., & van Sinderen, D. (2014) · FEMS Microbiology Reviews · doi:10.1111/1574-6976.12074 · Cited by 74
Regulation of themetC-cysKOperon, Involved in Sulfur Metabolism inLactococcus lactis
Fernández, M., Kleerebezem, M., Kuipers, O. P., Siezen, R. J., & van Kranenburg, R. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.1.82-90.2002 · Cited by 74
Self-citation
Contribution of Citrate Metabolism to the Growth of Lactococcus lactis CRL264 at Low pH
Sánchez, C., Neves, A. R., Cavalheiro, J. M. B. T., dos Santos, M. M., García-Quintáns, N., López, P., & Santos, H. (2007) · Applied and Environmental Microbiology · doi:10.1128/aem.01061-07 · Cited by 74
Genomic Evolution of Domesticated Microorganisms
Douglas, G. L., & Klaenhammer, T. R. (2010) · Annual Review of Food Science and Technology · doi:10.1146/annurev.food.102308.124134 · Cited by 74
Decrease in Penicillin Susceptibility Due to Heat Shock Protein ClpL in Streptococcus pneumoniae
Tran, T. D., Kwon, H., Kim, E., Kim, K.-W., Briles, D. E., Pyo, S., & Rhee, D. (2011) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01383-10 · Cited by 73
Transcriptional response of Streptococcus pneumoniae to Zn2+ limitation and the repressor/activator function of AdcR
Shafeeq, S., Kloosterman, T. G., & Kuipers, O. P. (2011) · Metallomics · doi:10.1039/c1mt00030f · Cited by 73
New Expression System Tightly Controlled by Zinc Availability in Lactococcus lactis
Llull, D., & Poquet, I. (2004) · Applied and Environmental Microbiology · doi:10.1128/aem.70.9.5398-5406.2004 · Cited by 73
Lactococcus lactis, a bacterial model for stress responses and survival
Duwat, P., Cesselin, B., Sourice, S., & Gruss, A. (2000) · International Journal of Food Microbiology · doi:10.1016/s0168-1605(00)00179-3 · Cited by 72
Characterization of the CtsR Stress Response Regulon in Lactobacillus plantarum
Fiocco, D., Capozzi, V., Collins, M., Gallone, A., Pascal Hols, A., Guzzo, J., Weidmann, S., Rieu, A., Msadek, T., & Spano, G. (2009) · Journal of Bacteriology · doi:10.1128/jb.01122-09 · Cited by 72
Osmotic response in Lactobacillus casei ATCC 393: biochemical and biophysical characteristics of membrane
Machado, M. C., López, C. S., Heras, H., & Rivas, E. A. (2003) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2003.11.001 · Cited by 71
Modification of the Technical Properties of Lactobacillus johnsonii NCC 533 by Supplementing the Growth Medium with Unsaturated Fatty Acids
Muller, J. A., Ross, R. P., Sybesma, W., Fitzgerald, G. F., & Stanton, C. (2011) · Applied and Environmental Microbiology · doi:10.1128/aem.05213-11 · Cited by 71
Self-citation
Contribution of a PerR-like regulator to the oxidative-stress response and virulence of Enterococcus faecalis
Verneuil, N., Rincé, A., Sanguinetti, M., Posteraro, B., Fadda, G., Auffray, Y., Hartke, A., & Giárd, J.-C. (2005) · Microbiology · doi:10.1099/mic.0.28325-0 · Cited by 71
Adaptation of the Wine Bacterium Oenococcus oeni to Ethanol Stress: Role of the Small Heat Shock Protein Lo18 in Membrane Integrity
Maitre, M., Weidmann, S., Dubois‐Brissonnet, F., David, V., Covès, J., & Guzzo, J. (2014) · Applied and Environmental Microbiology · doi:10.1128/aem.04178-13 · Cited by 71
Lowering GTP Level Increases Survival of Amino Acid Starvation but Slows Growth Rate for Bacillus subtilis Cells Lacking (p)ppGpp
Bittner, A. N., Kriel, A., & Wang, J. D. (2014) · Journal of Bacteriology · doi:10.1128/jb.01471-14 · Cited by 70
The groESL Chaperone Operon of Lactobacillus johnsonii
Walker, D. C., Girgis, H. S., & Klaenhammer, T. R. (1999) · Applied and Environmental Microbiology · doi:10.1128/aem.65.7.3033-3041.1999 · Cited by 70
Adaptation to high salt in Lactobacillus: role of peptides and proteolytic enzymes
Piuri, M., Sánchez-Rivas, C., & Ruzal, S. M. (2003) · Journal of Applied Microbiology · doi:10.1046/j.1365-2672.2003.01971.x · Cited by 69
Inactivation of the CovR/S Virulence Regulator Impairs Infection in an Improved Murine Model of Streptococcus pyogenes Naso-Pharyngeal Infection
Alam, F. M., Turner, C. E., Smith, K. C., Wiles, S., & Sriskandan, S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0061655 · Cited by 68
Identification and Characterization of a Bacitracin Resistance Network in Enterococcus faecalis
Gebhard, S., Fang, C., Shaaly, A., Leslie, D. J., Weimar, M. R., Kalamorz, F., Carne, A., & Cook, G. M. (2013) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02111-13 · Cited by 68

Research works printed but not linked: 3

Henick-Kling T, Cox DJ, Olsen EB. 1991. Production de l'energie durant la fermentation malolactique. Rev Fr Oenol 132:63–66.
Aprea G, Mullan WMA, Mullan A, Murru N, Tozzi M, Cortesi ML. 2005. Isolation of polyphosphate-accumulating lactic acid bacteria from natural whey starters. Milchwissenschaft 60:256–258.
Lim B, Gross CA. 2011. Cellular response to heat shock and cold shock, p 93–114. In Storz G, Hengge R (ed), Bacterial stress responses, 2nd ed. ASM Press, Washington, DC.

Sorted by citations

Metabolism Characteristics of Lactic Acid Bacteria and the Expanding Applications in Food Industry
Wang, Y., Wu, J., Lv, M., Shao, Z., Hungwe, M., Wang, J., Bai, X., Xie, J., Wang, Y., & Geng, W. (2021) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2021.612285 · Cited by 1,001
Microbial Fermentation and Its Role in Quality Improvement of Fermented Foods
Sharma, R., Garg, P., Kumar, P., Bhatia, S. K., & Kulshrestha, S. (2020) · Fermentation · doi:10.3390/fermentation6040106 · Cited by 824
The Lactobacillus casei group: history and health related applications
Hill, D., Sugrue, I., Tobin, C., Hill, C., Stanton, C., & Ross, R. P. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.02107 · Cited by 318
Self-citation
Tumor-resident Lactobacillus iners confer chemoradiation resistance through lactate-induced metabolic rewiring
Colbert, L. E., Alam, M. B. E., Wang, R., Karpinets, T. V., Lo, D., Lynn, E. J., Harris, T. A., Elnaggar, J. H., Yoshida-Court, K., Tomasic, K., et al. (2023) · Cancer Cell · doi:10.1016/j.ccell.2023.09.012 · Cited by 286
Bacterial exopolysaccharides as emerging bioactive macromolecules: from fundamentals to applications
Kaur, N., & Dey, P. (2022) · Research in Microbiology · doi:10.1016/j.resmic.2022.104024 · Cited by 285

See all 916

Authors: Papadimitriou, K., Alegría, Á., Bron, P. A., de Angelis, M., Gobbetti, M., Kleerebezem, M., Lemos, J. A., Linares, D. M., Ross, P., Stanton, C., Turroni, F., van Sinderen, D., Varmanen, P., Ventura, M., Zúñiga, M., Tsakalidou, E., & Kok, J.
Affiliations: Agricultural University of Athens (GR)
University of Groningen (NL)
TiFN (NL)
Department of Soil, Plant and Food Sciences, University of Bari Aldo Moro, Bari, Italy
University of Bari Aldo Moro (IT)
Department of Oral Biology, University of Florida College of Dentistry, Gainesville, Florida, USA
Teagasc - The Irish Agriculture and Food Development Authority (IE)
APC, Microbiome Institute, University College Cork, Cork, Ireland
University of Parma (IT)
University of Helsinki (FI)
Consejo Superior de Investigaciones Científicas (ES)
ORCID: Papadimitriou, Konstantinos
Alegría, Ángel
Bron, Peter A.
Gobbetti, Marco
Kleerebezem, Michiel
Stanton, Catherine
Turroni, Francesca
Varmanen, Pekka
Ventura, Marco
Zúñiga, Manuel
Tsakalidou, Effie
Kok, Jan
Venue: Microbiology and Molecular Biology Reviews
Publisher: American Society for Microbiology
Published: 2016-09
Volume: 80
Issue: 3
Pages: 837-890
ISSN: 1092-2172 (ISSN-L)
1098-5557
DOI: 10.1128/mmbr.00076-15
PMC: PMC4981675
OpenAlex: W2499564842
Cited by: 914
References: 646
Citations by year: 2026: 173 · 2025: 163 · 2024: 97 · 2023: 92 · 2022: 86 · 2021: 92 · 2020: 83 · 2019: 56 · 2018: 48 · 2017: 20 · 2016: 3
FWCI: 4.84
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Microbiology and Molecular Biology Reviews (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Socio-Environmental Systems Modeling (acceptedVersion)
CINECA IRIS Institutional Research Information System (University of Bari Aldo Moro) (submittedVersion, cc-by-nc-nd)
University of Groningen research database (University of Groningen / Centre for Information Technology) (submittedVersion, other-oa)
Open Research (University of Surrey) (submittedVersion)
Data Archiving and Networked Services (DANS) (submittedVersion)
Funders: European Commission (2007–2013, FP7 2007-2013, FP7/2007, 623448)
Science Foundation Ireland (13/IA/1953, 12/RC/2273, 12/RC/)
APC Microbiome Institute
National Institute of Dental and Craniofacial Research (DE019783, DE022559, R01DE019783, R01DE022559)
Topics: Life Sciences › Agricultural and Biological Sciences › Food Science › Probiotics and Fermented Foods
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Microbial Inactivation Methods
Keywords: lactic acid bacteria, stress physiology, stress response, probiotics, Lactobacillus, Lactococcus lactis, Enterococcus, Streptococcus, stress tolerance, biofilm, dormancy, prophage induction, stress tolerance engineering, food industry
MeSH terms: Energy Metabolism, Fermentation, Food Microbiology, Lactobacillus, Osmotic Pressure, Streptococcus, Stress, Physiological, Signal Transduction, Enterococcus, Biofilms, Lactic Acid, Probiotics

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Stress Physiology of Lactic Acid Bacteria.

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks