Antifungal activity of the Enterococcus faecalis peptide EntV requires protease cleavage and disulfide bond formation
Open accessAbstract
Enterococcus faecalis and Candida albicans are among the most important and problematic pathobionts, organisms that normally are harmless commensals but can cause dangerous infections in immunocompromised hosts. In fact, both organisms are listed by the Centers for Disease Control and Prevention as serious global public health threats stemming from the increased prevalence of antimicrobial resistance. The rise in antifungal resistance is of particular concern considering the small arsenal of currently available therapeutics. EntV is a peptide with antifungal properties, and it, or a similar compound, could be developed into a therapeutic alternative, either alone or in combination with existing agents. However, to do so requires understanding what properties of EntV are necessary for its antifungal activity. In this work, we studied the posttranslational processing of EntV and what modifications are necessary for inhibition of C. albicans in order to fill this gap in knowledge.
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
Cites
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?
The effect of E. faecalis on C. albicans is associated with a signaling event in which a bacterial-derived product, identified as EntV, a bacteriocin produced by E. faecalis as a pre-pro-peptide, inhibits C. albicans filamentation and biofilm formation.
“This effect was associated with a signaling event in which a bacterial-derived product inhibited C. albicans filamentation and biofilm formation, with subsequent studies identifying this product as EntV, a bacteriocin produced by E. faecalis as a pre-pro-peptide.”
From Antifungal therapy of Candida biofilms: Past, present and future (2023) · cites this paper as [60]
The active form of EntV is 68 amino acids, does not exhibit antifungal activity per se, and inhibits C. albicans biofilm formation both in vitro and in vivo.
“The active form of EntV is 68 amino acids [60], which per se does not exhibit antifungal activity, inhibits C. albicans biofilm formation both in vitro and in vivo [61].”
From Antifungal therapy of Candida biofilms: Past, present and future (2023) · cites this paper as [60]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Schägger, H., & von Jagow, G. (1987) · Analytical Biochemistry · doi:10.1016/0003-2697(87)90587-2 · Cited by 11,420 · see citing works
Nonfilamentous C. albicans Mutants Are Avirulent
Lo, H.-J., Köhler, J. R., DiDomenico, B., Loebenberg, D., Cacciapuoti, A., & Fink, G. R. (1997) · Cell · doi:10.1016/s0092-8674(00)80358-x · Cited by 1,809 · see citing works
Mayr, F., Yende, S. P., & Angus, D. C. (2013) · Virulence · doi:10.4161/viru.27372 · Cited by 1,251 · see citing works
<i>Candida albicans</i> Biofilms and Human Disease
Nobile, C. J., & Johnson, A. D. (2015) · Annual Review of Microbiology · doi:10.1146/annurev-micro-091014-104330 · Cited by 1,057 · see citing works
Enterococci: From Commensals to Leading Causes of Drug Resistant Infection
Gilmore, M. S., Clewell, D. B., Ike, Y., & Shankar, N. (2014) · Cited by 794 · see citing works
Polymicrobial Interactions: Impact on Pathogenesis and Human Disease
Peters, B. M., Jabra‐Rizk, M. A., O’May, G. A., Costerton, J. W., & Shirtliff, M. E. (2012) · Clinical Microbiology Reviews · doi:10.1128/cmr.00013-11 · Cited by 713 · see citing works
Saville, S. P., Lazzell, A. L., Monteagudo, C., & Lopez-Ribot, J. L. (2003) · Eukaryotic Cell · doi:10.1128/ec.2.5.1053-1060.2003 · Cited by 655 · see citing works
Medically important bacterial-fungal interactions
Peleg, A. Y., Hogan, D. A., & Mylonakis, E. (2010) · Nature Reviews Microbiology · doi:10.1038/nrmicro2313 · Cited by 619 · see citing works
Pseudomonas - Candida Interactions: An Ecological Role for Virulence Factors
Hogan, D. A., & Kolter, R. (2002) · Science · doi:10.1126/science.1070784 · Cited by 580 · see citing works
The enterococci : pathogenesis, molecular biology, and antibiotic resistance
Gilmore, M. S., & Clewell, D. B. (2002) · ASM eBooks · Cited by 461 · see citing works
Proteinases of common pathogenic bacteria degrade and inactivate the antibacterial peptide LL‐37
Schmidtchen, A., Frick, I.-M., Andersson, E., Tapper, H., & Björck, L. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.03146.x · Cited by 440 · see citing works
Qin, X., Singh, K. V., Weinstock, G. M., & Murray, B. E. (2000) · Infection and Immunity · doi:10.1128/iai.68.5.2579-2586.2000 · Cited by 364 · see citing works
Self-citationRamage, G., VandeWalle, K., López-Ribot, J. L., & Wickes, B. L. (2002) · FEMS Microbiology Letters · doi:10.1016/s0378-1097(02)00853-4 · Cited by 334 · see citing works
Antifungal Chemical Compounds Identified Using a C. elegans Pathogenicity Assay
Breger, J. A., Fuchs, B. B., Aperis, G., Moy, T. I., Ausubel, F. M., & Mylonakis, E. E. (2007) · PLoS Pathogens · doi:10.1371/journal.ppat.0030018 · Cited by 334 · see citing works
Thomas, V. C., Thurlow, L. R., Boyle, D., & Hancock, L. E. (2008) · Journal of Bacteriology · doi:10.1128/jb.00314-08 · Cited by 302 · see citing works
Bamford, C. V., d'Mello, A., Nobbs, A. H., Dutton, L. C., Vickerman, M. M., & Jenkinson, H. F. (2009) · Infection and Immunity · doi:10.1128/iai.00438-09 · Cited by 291 · see citing works
Peters, B. M., Jabra‐Rizk, M. A., Scheper, M. A., Leid, J. G., Costerton, J. W., & Shirtliff, M. E. (2010) · FEMS Immunology & Medical Microbiology · doi:10.1111/j.1574-695x.2010.00710.x · Cited by 288 · see citing works
Klotz, S. A., Chasin, B. S., Powell, B., Gaur, N. K., & Lipke, P. N. (2007) · Diagnostic Microbiology and Infectious Disease · doi:10.1016/j.diagmicrobio.2007.07.001 · Cited by 252 · see citing works
Fungal Biofilms, Drug Resistance, and Recurrent Infection
Desai, J. V., Mitchell, A. P., & Andes, D. R. (2014) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a019729 · Cited by 252 · see citing works
Control of Candida albicans Metabolism and Biofilm Formation by Pseudomonas aeruginosa Phenazines
Morales, D. K., Grahl, N., Okegbe, C., Dietrich, L. E. P., Jacobs, N. J., & Hogan, D. A. (2013) · mBio · doi:10.1128/mbio.00526-12 · Cited by 241 · see citing works
Dutton, R. J., Boyd, D. H., Berkmen, M., & Beckwith, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0804621105 · Cited by 239 · see citing works
Graham, C. E., Cruz, M. R., Garsin, D. A., & Lorenz, M. C. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1620432114 · Cited by 239 · see citing works
Self-citationSifri, C. D., Mylonakis, E. E., Singh, K. V., Qin, X., Garsin, D. A., Murray, B. E., Ausubel, F. M., & Calderwood, S. B. (2002) · Infection and Immunity · doi:10.1128/iai.70.10.5647-5650.2002 · Cited by 222 · see citing works
Self-citationGeneration and Testing of Mutants ofEnterococcus faecalisin a Mouse Peritonitis Model
Singh, K. V., Qin, X., Weinstock, G. M., & Murray, B. E. (1998) · The Journal of Infectious Diseases · doi:10.1086/314453 · Cited by 208 · see citing works
Self-citationMurray, B. E., Singh, K. V., Ross, R. P., Heath, J. D., Dunny, G. M., & Weinstock, G. M. (1993) · Journal of Bacteriology · doi:10.1128/jb.175.16.5216-5223.1993 · Cited by 203 · see citing works
Self-citationThomas, V. C., Hiromasa, Y., Harms, N., Thurlow, L., Tomich, J., & Hancock, L. E. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06703.x · Cited by 197 · see citing works
Enterococcus faecalis inhibits hyphal morphogenesis and virulence of Candida albicans
Cruz, M. R., Graham, C. E., Gagliano, B. C., Lorenz, M. C., & Garsin, D. A. (2013) · Infection and Immunity · doi:10.1128/iai.00914-12 · Cited by 188 · see citing works
Self-citationKristich, C. J., Chandler, J. R., & Dunny, G. M. (2006) · Plasmid · doi:10.1016/j.plasmid.2006.08.003 · Cited by 187 · see citing works
Schmidtchen, A., Frick, I.-M., & Björck, L. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02251.x · Cited by 160 · see citing works
Mäkinen, P. ‐., Clewell, D. B., An, F. Y., & Mäkinen, K. K. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94069-x · Cited by 152 · see citing works
Summers, K. L., Erb‐Downward, J. R., Falkowski, N. R., Young, V. B., Kao, J. Y., & Huffnagle, G. B. (2011) · Infection and Immunity · doi:10.1128/iai.05162-11 · Cited by 151 · see citing works
Disulfide bond formation in prokaryotes
Landeta, C., Boyd, D., & Beckwith, J. (2018) · Nature Microbiology · doi:10.1038/s41564-017-0106-2 · Cited by 135 · see citing works
(2002) · ASM Press eBooks · doi:10.1128/9781555817923 · Cited by 132 · see citing works
MacCallum, W. G., & Hastings, T. W. (1899) · The Journal of Experimental Medicine · doi:10.1084/jem.4.5-6.521 · Cited by 130 · see citing works
Thiol-Disulfide Oxidoreductases Are Essential for the Production of the Lantibiotic Sublancin 168
Dorenbos, R., Stein, T. H., Kabel, J., Bruand, C., Bolhuis, A., Bron, S., Quax, W. J., & van Dijl, J. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201158200 · Cited by 116 · see citing works
Enterococcal Bacteremia: Analysis of 75 Episodes
Gullberg, R. M., Homann, S. R., & Phair, J. (1989) · Clinical Infectious Diseases · doi:10.1093/clinids/11.1.74 · Cited by 114 · see citing works
Disulfide Bond Formation and Cysteine Exclusion in Gram-positive Bacteria
Daniels, R., Mellroth, P., Bernsel, A., Neiers, F., Normark, S. J., von HEIJNE, G., & Henriques‐Normark, B. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.081398 · Cited by 93 · see citing works
Zeng, J., Teng, F., & Murray, B. E. (2005) · Infection and Immunity · doi:10.1128/iai.73.3.1606-1612.2005 · Cited by 93 · see citing works
Self-citationThiol‐disulphide oxidoreductase modules in the low‐GC Gram‐positive bacteria
Kouwen, T. R. H. M., van der Goot, A., Dorenbos, R., Winter, T., Antelmann, H., Plaisier, M., Quax, W. J., van Dijl, J. M., & Dubois, J. F. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.05707.x · Cited by 81 · see citing works
Archived polyacrylamide gels as a resource for proteome characterization by mass spectrometry
Shevchenko, A., Loboda, A., Ens, W., Schraven, B. L., Standing, K. G., & Shevchenko, A. (2001) · Electrophoresis · doi:10.1002/1522-2683()22:6 · Cited by 76 · see citing works
Enterocin F4-9, a Novel O -Linked Glycosylated Bacteriocin
Maky, M. A., Ishibashi, N., Zendo, T., Pérez, R., R, J. R. D. P. M., Karmi, M., & Sonomoto, K. (2015) · Applied and Environmental Microbiology · doi:10.1128/aem.00940-15 · Cited by 75 · see citing works
Pinkston, K. L., Gao, P., Garcia, D. D., Sillanpää, J., Nallapareddy, S. R., Murray, B. E., & Harvey, B. R. (2011) · Journal of Bacteriology · doi:10.1128/jb.05026-11 · Cited by 75 · see citing works
Self-citationBacterial flora accompanying Candida yeasts in clinical specimens
Hermann, C. A., Hermann, J., Munzel, U., & Rüchel, R. (1999) · Mycoses · doi:10.1046/j.1439-0507.1999.00519.x · Cited by 74 · see citing works
Disulfide-Bond-Forming Pathways in Gram-Positive Bacteria
Reardon‐Robinson, M. E., & Ton‐That, H. (2015) · Journal of Bacteriology · doi:10.1128/jb.00769-15 · Cited by 72 · see citing works
Enterococcus faecalis Mutations Affecting Virulence in the Caenorhabditis elegans Model Host
Maadani, A., Fox, K. A., Mylonakis, E., & Garsin, D. A. (2007) · Infection and Immunity · doi:10.1128/iai.01372-06 · Cited by 71 · see citing works
Self-citationCandida albicansandEnterococcus faecalisin the gut
Garsin, D. A., & Lorenz, M. C. (2013) · Gut Microbes · doi:10.4161/gmic.26040 · Cited by 60 · see citing works
Self-citationTwo Allelic Forms of the Aureolysin Gene ( aur ) within Staphylococcus aureus
Sabat, A. J., Kosowska, K., Poulsen, K., Kasprowicz, A., Sekowska, A., van den Burg, B., Travis, J. W., & Potempa, J. (2000) · Infection and Immunity · doi:10.1128/iai.68.2.973-976.2000 · Cited by 58 · see citing works
Dumoulin, A., Grauschopf, U., Bischoff, M., Thöny‐Meyer, L., & Berger‐Bächi, B. (2005) · Archives of Microbiology · doi:10.1007/s00203-005-0024-1 · Cited by 53 · see citing works
Full Activation of Enterococcus faecalis Gelatinase by a C-Terminal Proteolytic Cleavage
Papa, M. F. D., Hancock, L. E., Thomas, V. C., & Perego, M. (2007) · Journal of Bacteriology · doi:10.1128/jb.01311-07 · Cited by 50 · see citing works
Polymicrobial Bloodstream Infection in Pediatric Patients
Sutter, D. E., Stagliano, D. R., Braun, L. E., Williams, F., Arnold, J. C., Ottolini, M. G., & Epstein, J. (2008) · The Pediatric Infectious Disease Journal · doi:10.1097/inf.0b013e31816591be · Cited by 47 · see citing works
Staab, J. F., Bahn, Y., & Sundstrom, P. (2003) · Microbiology · doi:10.1099/mic.0.26445-0 · Cited by 47 · see citing works
O’Donohue, M. J., Roques, B. P., & Beaumont, A. (1994) · Biochemical Journal · doi:10.1042/bj3000599 · Cited by 46 · see citing works
Dundar, H., Brede, D. A., Rosa, S. L. L., EL-Gendy, A. O., Diep, D. B., & Nes, I. F. (2015) · Journal of Bacteriology · doi:10.1128/jb.02513-14 · Cited by 45 · see citing works
Swe, P. M., Heng, N. C. K., Ting, Y. T., Baird, H. J., Carne, A., Tauch, A., Tagg, J. R., & Jack, R. W. (2007) · Microbiology · doi:10.1099/mic.0.2007/010777-0 · Cited by 25 · see citing works
van der Kooi‐Pol, M. M., Reilman, E., Sibbald, M. J. J. B., Veenstra‐Kyuchukova, Y. K., Kouwen, T. R. H. M., Buist, G., & van Dijl, J. M. (2012) · Applied and Environmental Microbiology · doi:10.1128/aem.01565-12 · Cited by 18 · see citing works
Isolation and Characterization of Plasmids Carrying the dut Gene of Escherichia coli.
LUNDBERG, L. G., Nyman, P. O., Karlström, O. H., Nishida, T., Enzell, C. R., Rosell, S., Yanaihara, N., & Yanaihara, C. (1979) · Acta chemica Scandinavica/Acta chemica Scandinavica. B, Organic chemistry and biochemistry/Acta chemica Scandinavica. A, Physical and inorganic chemistry/Acta chemica Scandinavica. Series B. Organic chemistry and biochemistry/Acta chemica Scandinavica. Series A, Physical and inorganic chemistry · doi:10.3891/acta.chem.scand.33b-0597 · Cited by 9 · see citing works
Gilmore, M. S., Clewell, D. B., Ike, Y., & Shankar, N. (2014) · Cited by 6 · see citing works
Structure of Conserved Protein of Unknown Function from Enterococcus faecalis V583
Nocek, B. P., Li, H., Collart, F., Joachimiak, A., & MCSG (2005) · Worldwide Protein Data Bank · doi:10.2210/pdb1z6m/pdb · Cited by 2 · see citing works
Flagged first, then by citations
Research works printed but not linked: 1
- [30]Garsin DA, Frank KL, Silanpaa J, Ausubel FM, Hartke A, Shankar N, Murray BE 2014 Pathogenesis and models of enterococcal infection, p 185– 258. In Gilmore MS, Clewell DB, Ike Y, Shankar N (ed), Enterococci: from commensals to leading causes of drug resistant infection. Massachusetts Eye and Ear Infirmary, Boston, MA. 24649512
Cited by
Sorted by citations
Antimicrobial Peptides: a New Frontier in Antifungal Therapy
Cesare, G. B. D., Cristy, S. A., Garsin, D. A., & Lorenz, M. C. (2020) · mBio · doi:10.1128/mbio.02123-20 · Cited by 237 · see citing works
Self-citationCandida spp./Bacteria Mixed Biofilms
Rodrigues, M. E., Gomes, F., & Rodrigues, C. F. (2019) · Journal of Fungi · doi:10.3390/jof6010005 · Cited by 149 · see citing works
Zeise, K. D., Woods, R. J., & Huffnagle, G. B. (2021) · Clinical Microbiology Reviews · doi:10.1128/cmr.00323-20 · Cited by 101 · see citing works
The interplay between gut bacteria and the yeast Candida albicans
Pérez, J. C. (2021) · Gut Microbes · doi:10.1080/19490976.2021.1979877 · Cited by 74 · see citing works
Bacterial‐fungal interactions and their impact on microbial pathogenesis
MacAlpine, J., Robbins, N., & Cowen, L. E. (2022) · Molecular Ecology · doi:10.1111/mec.16411 · Cited by 72 · see citing works
Antimicrobial peptides: from discovery to developmental applications
Zhang, Q. (2025) · Applied and Environmental Microbiology · doi:10.1128/aem.02115-24 · Cited by 64 · see citing works
Microbiome assembly on Drosophila body surfaces benefits the flies to combat fungal infections
Song, H., Sun, Y., Sun, D., & Wang, C. (2022) · iScience · doi:10.1016/j.isci.2022.104408 · Cited by 64 · see citing works
Antifungal therapy of Candida biofilms: Past, present and future
Ajetunmobi, O. H., Badali, H., Romo, J. A., Ramage, G., & Lopez-Ribot, J. L. (2023) · Biofilm · doi:10.1016/j.bioflm.2023.100126 · Cited by 52 · see citing works
Song, H., Sun, Y., Chen, H., & Wang, C. (2022) · The ISME Journal · doi:10.1038/s41396-022-01323-7 · Cited by 52 · see citing works
Candida–bacterial cross-kingdom interactions
Eichelberger, K. R., Paul, S., Peters, B. M., & Cassat, J. E. (2023) · Trends in Microbiology · doi:10.1016/j.tim.2023.08.003 · Cited by 52 · see citing works
Candida albicans can foster gut dysbiosis and systemic inflammation during HIV infection
Zaongo, S. D., Ouyang, J., Isnard, S., Zhou, X., Harypursat, V., Cui, H., Routy, J., & Chen, Y. (2023) · Gut Microbes · doi:10.1080/19490976.2023.2167171 · Cited by 47 · see citing works
Mucosal Bacteria Modulate Candida albicans Virulence in Oropharyngeal Candidiasis
Bertolini, M., Vázquez-Muñoz, R., Archambault, L. S., Shah, S., Souza, J. G. S., Costa, R. C., Thompson, A. K., Zhou, Y., Sobue, T., & Dongari‐Bagtzoglou, A. I. (2021) · mBio · doi:10.1128/mbio.01937-21 · Cited by 43 · see citing works
Fasusi, O. A., Amoo, A. E., & Babalola, O. O. (2021) · Antonie van Leeuwenhoek · doi:10.1007/s10482-021-01633-4 · Cited by 33 · see citing works
Cruz, M. R., Cristy, S., Guha, S., De Cesare, G. B., Evdokimova, E., Sanchez, H., Borek, D., Miramón, P., Yano, J., Fidel, P. L., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-33613-1 · Cited by 30 · see citing works
Self-citationHuang, J., Lou, Y., Liu, J., Bulet, P., Cai, C., Ma, K., Jiao, R., Hoffmann, J. A., Liégeois, S., Li, Z., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2205140120 · Cited by 30 · see citing works
Candida albicans and Enterococcus faecalis biofilm frenemies: When the relationship sours
Alshanta, O. A., Albashaireh, K. Z., McKloud, E., Delaney, C., Kean, R., McLean, W., & Ramage, G. (2022) · Biofilm · doi:10.1016/j.bioflm.2022.100072 · Cited by 29 · see citing works
Cardiac Microlesions Form During Severe Bacteremic Enterococcus faecalis Infection
Brown, A. O., Singh, K. V., Cruz, M. R., Kaval, K. G., Francisco, L. E., Murray, B. E., & Garsin, D. A. (2020) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiaa371 · Cited by 24 · see citing works
Self-citationJiang, M., Dong, F.-Y., Pan, X., Zhang, Y., & Zhang, F. (2020) · Pesticide Biochemistry and Physiology · doi:10.1016/j.pestbp.2020.104756 · Cited by 22 · see citing works
Demin, K. A., Refeld, A. G., Bogdanova, A. A., Prazdnova, E. V., Popov, I. V., Kutsevalova, O. Y., Ermakov, A. M., Bren, A. B., Rudoy, D. V., Chistyakov, V. A., et al. (2021) · Probiotics and Antimicrobial Proteins · doi:10.1007/s12602-021-09776-6 · Cited by 24 · see citing works
Erriah, P., Puan, S. L., Normi, Y. M., Kamil, W. N. I. W. A., Nordin, S. A., Muhamad, A., & Sabri, S. (2024) · Journal of Applied Microbiology · doi:10.1093/jambio/lxae290 · Cited by 19 · see citing works
Willett, J. L. E., Robertson, E. B., & Dunny, G. M. (2022) · Journal of Bacteriology · doi:10.1128/jb.00129-22 · Cited by 18 · see citing works
Bacillus Metabolites: Compounds, Identification and Anti-Candida albicans Mechanisms
Wang, W., Zhao, J., & Zhang, Z. (2022) · Microbiology Research · doi:10.3390/microbiolres13040070 · Cited by 13 · see citing works
Optimization of the antifungal properties of the bacterial peptide EntV by variant analysis
Guha, S., Cristy, S. A., Cesare, G. B. D., Cruz, M. R., Lorenz, M. C., & Garsin, D. A. (2024) · mBio · doi:10.1128/mbio.00570-24 · Cited by 10 · see citing works
Self-citationHuang, D., Li, H., Lin, Y., Lin, J., Li, C., Kuang, Y., Zhou, W. J., Huang, B. S., & Wang, P. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.981823 · Cited by 10 · see citing works
Impact of the host microbiota on fungal infections: New possibilities for intervention?
Chow, E. W. L., Pang, L. M., & Wang, Y. (2023) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2023.114896 · Cited by 9 · see citing works
Huang, J., Lou, Y., Liu, J., Bulet, P., Jiao, R., Hoffmann, J. A., Liégeois, S., Li, Z., & Ferrandon, D. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.11.23.394809 · Cited by 8 · see citing works
Unveiling the fungal frontier: mycological insights into inflammatory bowel disease
Chen, S., Yi, M., Yi, X., Zhou, Y., Song, H., & Zeng, M. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1551289 · Cited by 10 · see citing works
Enterococcal quorum-controlled protease alters phage infection
Sheriff, E. K., Salvato, F., Andersen, S. E., Chatterjee, A., Kleiner, M., & Duerkop, B. A. (2024) · FEMS Microbes · doi:10.1093/femsmc/xtae022 · Cited by 6 · see citing works
Systems biology of host-Candida interactions: understanding how we shape each other
Hodgins-Davis, A., & O’Meara, T. R. (2020) · Current Opinion in Microbiology · doi:10.1016/j.mib.2020.04.001 · Cited by 5 · see citing works
Impact of interkingdom microbial interactions in the vaginal tract
Cohen, S., Ost, K. S., & Doran, K. S. (2024) · PLoS Pathogens · doi:10.1371/journal.ppat.1012018 · Cited by 7 · see citing works
Multispecies oral biofilm and identification of components as treatment target
Velázquez-Moreno, S., Zavala-Alonso, N. V., Rodríguez, R. O., Quintana, M., Ojeda‐Galván, H. J., González‐Ortega, O., & Martínez‐Gutiérrez, F. (2023) · Archives of Oral Biology · doi:10.1016/j.archoralbio.2023.105821 · Cited by 5 · see citing works
Evaluation of functional properties of lactic acid bacteria isolated from traditional cheese
Mohammed, S., Özdemir, N., & Çon, A. H. (2024) · Measurement Food · doi:10.1016/j.meafoo.2024.100171 · Cited by 4 · see citing works
The pathogenesis of cardiac microlesion formation during severe bacteremic infection
Brown, A. O., & Garsin, D. A. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1009021 · Cited by 4 · see citing works
Self-citationFong, J. L., Yong, V. O. E., Yeo, C., Adamson, C., Li, L., Zhang, D., & Qiao, Y. (2024) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.4c00515 · Cited by 4 · see citing works
The disulfide bond formation (DSB) system: so much more than a housekeeper
Kadeřábková, N., & Mavridou, D. A. I. (2025) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/bs.ampbs.2025.07.002 · Cited by 3 · see citing works
Tanoto, F. R., Liew, J. H., Stocks, C. J., Rawat, D., Chong, K., Pethe, K., Antypas, H., & Kline, K. A. (2026) · PLoS Pathogens · doi:10.1371/journal.ppat.1013738 · Cited by 3 · see citing works
Zhang, X., Yang, L., Cai, T., Liao, H., Cai, P., Zhao, X., Gu, N., Yue, Z., Gu, Y., Zhang, F., et al. (2025) · BMC Microbiology · doi:10.1186/s12866-025-03980-y · Cited by 3 · see citing works
Robertson, E. B., & Willett, J. L. E. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.09.12.557362 · Cited by 3 · see citing works
Opportunities in exploring chemical biology tools for better strategies against Candida albicans
Li, L., & Qiao, Y. (2025) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2025.102595 · Cited by 1 · see citing works
Cesare, G. B. D., Cruz, M. R., Cristy, S. A., Vega, L. A., Żarnowski, R., Zito, A., Guha, S., Andes, D. R., Garsin, D. A., & Lorenz, M. C. (2025) · PLoS Pathogens · doi:10.1371/journal.ppat.1013519 · Cited by 1 · see citing works
Self-citationVázquez-Muñoz, R., Ranjan, A. K., Bertolini, M., Thompson, A. M., Ghahfarokhy, P. M., Harnden, A., Nobile, C. J., Sobue, T., Vera‐Licona, P., & Dongari‐Bagtzoglou, A. I. (2025) · mSphere · doi:10.1128/msphere.00822-25 · Cited by 1 · see citing works
Recurring principles of metabolic interactions in Enterococcus faecalis polymicrobial communities
Anderson, C. M., & Kline, K. A. (2026) · Current Opinion in Microbiology · doi:10.1016/j.mib.2026.102796 · Cited by 1 · see citing works
Isenberg, R. Y., Sackih, C. W., & Willett, J. L. E. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.07.31.667707 · Cited by 1 · see citing works
Mäkinen, K. K., & Mäkinen, P. (2025) · Handbook of Proteolytic Enzymes · doi:10.1016/b978-0-443-28849-4.00039-4
Wang, J., Chen, H., & Tang, J. (2026) · Microbiological Research · doi:10.1016/j.micres.2026.128654
Streptococcal mutanobactin mediates interspecies competition with gram-positive bacteria
Isenberg, R. Y., Sackih, C. W., Abdulrahman, F. A., & Willett, J. L. E. (2026) · mBio · doi:10.1128/mbio.01623-26
- Authors
- Brown, A. O., Graham, C. E., Cruz, M. R., Singh, K. V., Murray, B. E., Lorenz, M. C., & Garsin, D. A.
- Affiliations
- The University of Texas Health Science Center at Houston (US)
- The University of Texas MD Anderson Cancer Center (US)
- Corresponding author
- Garsin, Danielle A.
- ORCID
- Venue
- mBio
- Publisher
- American Society for Microbiology
- Published
- 2019-08-27
- Volume
- 10
- Issue
- 4
- ISSN
- 2150-7511 (ISSN-L)
- 2161-2129
- PMC
- PMC6606811
- OpenAlex
- W2956045308
- Cited by
- 46
- References
- 58
- Citations by year
- 2026: 4 · 2025: 9 · 2024: 6 · 2023: 7 · 2022: 8 · 2021: 5 · 2020: 6 · 2019: 1
- FWCI
- 3.67
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- mBio (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- HHS | NIH | National Institute of Allergy and Infectious Diseases (F31AI122725)
- HHS | NIH | National Institute of Dental and Craniofacial Research (R01DE027608, F32DE027580)
- Topics
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Health Sciences › Medicine › Pharmacology › Microbial Natural Products and Biosynthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Keywords
- Enterococcus faecalis, Candida albicans, antifungal activity, protease cleavage, disulfide bond formation, post-translational processing, pathobionts, antifungal resistance, antimicrobial peptides
- MeSH terms
- Antifungal Agents, Bacteriocins, Candida albicans, Disulfides, Protein Processing, Post-Translational, Enterococcus faecalis, Gelatinases, Hyphae, Proteolysis
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