Salmonella enterica Serovar Typhimurium HtrA: regulation of expression and role of the chaperone and protease activities during infection
Abstract
HtrA is a bifunctional stress protein required by many bacterial pathogens to successfully cause infection. Salmonella enterica serovar Typhimurium (S. Typhimurium) htrA mutants are defective in intramacrophage survival and are highly attenuated in mice. Transcription of htrA in Escherichia coli is governed by a single promoter that is dependent on σ E (RpoE). S. Typhimurium htrA also possesses a σ E-dependent promoter; however, we found that the absence of σ E had little effect on production of HtrA by S. Typhimurium. This suggests that additional promoters control expression of htrA in S. Typhimurium. We identified three S. Typhimurium htrA promoters. Only the most proximal promoter, htrAp3, was σ E dependent. The other promoters, htrAp1 and htrAp2, are probably recognized by the principal sigma factor σ 70. These two promoters were constitutively expressed but were also slightly induced by heat shock. Thus expression of htrA is different in S. Typhimurium and E. coli. The role of HtrA is to deal with misfolded/damaged proteins in the periplasm. It can do this either by degrading (protease activity) or folding/capturing (chaperone/sequestering, C/S, activity) the aberrant protein. We investigated which of these functions are important to S. Typhimurium in vitro and in vivo. Point or deletion mutants of htrA that encode variant HtrA molecules have been used in previous studies to investigate the role of different regions of HtrA in C/S and protease activity. These htrA variants were placed under the control of the S. Typhimurium htrAP123 promoters and expressed in a S. Typhimurium htrA mutant, GVB1343. Both wild-type HtrA and HtrA (HtrA S210A) lacking protease activity enabled GVB1343 to grow at high temperature (46 °C). Both molecules also significantly enhanced the growth/survival of GVB1343 in the liver and spleen of mice during infection. However, expression of wild-type HtrA enabled GVB1343 to grow to much higher levels than expression of HtrA S210A. Thus both the protease and C/S functions of HtrA operate in vivo during infection but the protease function is probably more important. Absence of either PDZ domain completely abolished the ability of HtrA to complement the growth defects of GVB1343 in vitro or in vivo.
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H. pylori, Salmonella typhimurium and Campylobacter jejuni interact with the host cell epithelium and establish infection by HtrA.
“As H. pylori, Salmonella typhimurium and Campylobacter jejuni, a bacterium responsible for foodborne infections, interact with the host cell epithelium and establish infection by HtrA.79–81”
From The emerging roles of bacterial proteases in intestinal diseases (2023) · cites this paper as [81]
Cites
Experiments in molecular genetics
Miller, J. H. (1972) · Medical Entomology and Zoology · Cited by 27,157 · see citing works
[57] Sequencing end-labeled DNA with base-specific chemical cleavages
Maxam, A. M., & Gilbert, W. (1980) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(80)65059-9 · Cited by 14,678 · see citing works
Aromatic-dependent Salmonella typhimurium are non-virulent and effective as live vaccines
Hoiseth, S. K., & Stocker, B. A. D. (1981) · Nature · doi:10.1038/291238a0 · Cited by 2,088 · see citing works
Wang, R. F., & Kushner, S. R. (1991) · Gene · doi:10.1016/0378-1119(91)90366-j · Cited by 1,178 · see citing works
Eriksson, S., Lucchini, S., Thompson, A., Rhen, M., & Hinton, J. C. D. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03313.x · Cited by 846 · see citing works
A Temperature-Dependent Switch from Chaperone to Protease in a Widely Conserved Heat Shock Protein
Spiess, C., Beil, A., & Ehrmann, M. (1999) · Cell · doi:10.1016/s0092-8674(00)80743-6 · Cited by 768 · see citing works
Nucleotide sequence of an RNA polymerase binding site at an early T7 promoter.
Pribnow, D. G. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.3.784 · Cited by 610 · see citing works
Conserved and Variable Functions of the σE Stress Response in Related Genomes
Rhodius, V. A., Suh, W.-C., Nonaka, G., West, J. T., & Gross, C. A. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0040002 · Cited by 521 · see citing works
The HtrA family of serine proteases
Pallen, M. J., & Wren, B. W. (1997) · Molecular Microbiology · doi:10.1046/j.1365-2958.1997.5601928.x · Cited by 396 · see citing works
HOW SALMONELLA SURVIVE AGAINST THE ODDS
Foster, J. W., & Spector, M. P. (1995) · Annual Review of Microbiology · doi:10.1146/annurev.mi.49.100195.001045 · Cited by 372 · see citing works
Structural basis for the regulated protease and chaperone function of DegP
Krojer, T. J., Sawa-Makarska, J. Z., Schäfer, E., Saibil, H. R., Ehrmann, M., & Clausen, T. (2008) · Nature · doi:10.1038/nature07004 · Cited by 368 · see citing works
Lipińska, B., Fayet, O., Baird, L. M., & Georgopoulos, C. P. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.3.1574-1584.1989 · Cited by 342 · see citing works
Danese, P. N., Snyder, W. B., Cosma, C. L., Davis, L. J., & Silhavy, T. J. (1995) · Genes & Development · doi:10.1101/gad.9.4.387 · Cited by 325 · see citing works
Pushing the envelope: extracytoplasmic stress responses in bacterial pathogens
Rowley, G., Spector, M. P., Kormanec, J., & Roberts, M. (2006) · Nature Reviews Microbiology · doi:10.1038/nrmicro1394 · Cited by 321 · see citing works
Self-citationPogliano, J., Lynch, A. S., Belin, D., Lin, E. C. C., & Beckwith, J. (1997) · Genes & Development · doi:10.1101/gad.11.9.1169 · Cited by 306 · see citing works
The role of a stress‐response protein in Salmonella typhimurium virulence
Johnson, K. S., Charles, I. G., Gordon Dougan, B., Pickard, D., Gaora, P. Ó., Costa, G., Ali, T., Miller, I. A., & Hormaeche, C. E. (1991) · Molecular Microbiology · doi:10.1111/j.1365-2958.1991.tb02122.x · Cited by 273 · see citing works
Lipińska, B., Sharma, S., & Georgopoulos, C. P. (1988) · Nucleic Acids Research · doi:10.1093/nar/16.21.10053 · Cited by 253 · see citing works
Salmonella typhimurium loci involved in survival within macrophages
Bäumler, A. J., Kusters, J. G., Stojiljković, I., & Heffron, F. (1994) · Infection and Immunity · doi:10.1128/iai.62.5.1623-1630.1994 · Cited by 241 · see citing works
Humphreys, S., Stevenson, A. W., Bacon, A. K., Weinhardt, A. B., & Roberts, M. (1999) · Infection and Immunity · doi:10.1128/.67.4.1560-1568.1999 · Cited by 236 · see citing works
Self-citationWulf, P. D., Manson, A. L., Liu, X., & Lin, E. C. C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203487200 · Cited by 221 · see citing works
Testerman, T. L., Vázquez‐Torres, A., Xu, Y., Jones‐Carson, J., Libby, S. J., & Fang, F. C. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.02787.x · Cited by 186 · see citing works
Jiang, J., Zhang, X., Chen, Y., Wu, Y., Zhou, Z. H., Chang, Z., & Sui, S. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805464105 · Cited by 160 · see citing works
Chatfield, S. N., Strahan, K. M., Pickard, D., Charles, I. G., Hormaeche, C. E., & Gordon Dougan, B. (1992) · Microbial Pathogenesis · doi:10.1016/0882-4010(92)90117-7 · Cited by 153 · see citing works
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 · see citing works
Bringer, M.-A., Barnich, N., Glasser, A.-L., Bardot, O., & Darfeuille–Michaud, A. (2005) · Infection and Immunity · doi:10.1128/iai.73.2.712-721.2005 · Cited by 104 · see citing works
Role of the htrA Gene in Klebsiella pneumoniae Virulence
Cortés, G., de Astorza, B., Benedi, V. J., & Albertí, S. (2002) · Infection and Immunity · doi:10.1128/iai.70.9.4772-4776.2002 · Cited by 90 · see citing works
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 · see citing works
Identification of the σ E regulon of Salmonella enterica serovar Typhimurium
Škovierová, H., Rowley, G., Řežuchová, B., Homerová, D., Lewis, C., Roberts, M., & Kormanec, J. (2006) · Microbiology · doi:10.1099/mic.0.28744-0 · Cited by 83 · see citing works
Self-citationPedersen, L. L., Radulic, M., Dorić, M., & Kwaik, Y. A. (2001) · Infection and Immunity · doi:10.1128/iai.69.4.2569-2579.2001 · Cited by 79 · see citing works
Misra, R., Castillo-Keller, M., & Deng, M. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.17.4882-4888.2000 · Cited by 77 · see citing works
Rigoulay, C., Entenza, J. M., Halpern, D., Widmer, E., Moreillon, P., Poquet, I., & Gruss, A. (2004) · Infection and Immunity · doi:10.1128/iai.73.1.563-572.2005 · Cited by 66 · see citing works
Miticka, H., Rowley, G., Řežuchová, B., Homerová, D., Humphreys, S., Farn, J., Roberts, M., & Kormanec, J. (2003) · FEMS Microbiology Letters · doi:10.1016/s0378-1097(03)00600-1 · Cited by 59 · see citing works
Self-citationEverest, P. H., Frankel, G. M., Li, J., Lund, P. A., Chatfield, S. N., & Gordon Dougan, B. (1995) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1995.tb07398.x · Cited by 59 · see citing works
Protease-Deficient DegP Suppresses Lethal Effects of a Mutant OmpC Protein by Its Capture
Castillo-Keller, M., & Misra, R. (2002) · Journal of Bacteriology · doi:10.1128/jb.185.1.148-154.2003 · Cited by 58 · see citing works
Kenyon, W. J., Sayers, D. G., Humphreys, S., Roberts, M., & Spector, M. P. (2002) · Microbiology · doi:10.1099/00221287-148-1-113 · Cited by 55 · see citing works
Self-citationAnalyzing the Developmental Expression of Sigma Factors with S1-Nuclease Mapping
Kormanec, J. (2003) · Humana Press eBooks · doi:10.1385/1-59259-233-3:481 · Cited by 55 · see citing works
Self-citationSkórko‐Glonek, J., Laskowska, E., Sobiecka-Szkatuła, A., & Lipińska, B. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.04.006 · Cited by 45 · see citing works
Role of Periplasmic Peptidylprolyl Isomerases in Salmonella enterica Serovar Typhimurium Virulence
Humphreys, S., Rowley, G., Stevenson, A., Kenyon, W. J., Spector, M. P., & Roberts, M. (2003) · Infection and Immunity · doi:10.1128/iai.71.9.5386-5388.2003 · Cited by 42 · see citing works
Self-citationInvestigation into the role of the serine protease HtrA in Yersinia pestis pathogenesis
Williams, K. J., Oyston, P. C. F., Dorrell, N., Li, S.-R., Titball, R. W., & Wren, B. W. (2000) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2000.tb09118.x · Cited by 40 · see citing works
Řežuchová, B., & Kormanec, J. (2001) · Journal of Microbiological Methods · doi:10.1016/s0167-7012(01)00237-8 · Cited by 36 · see citing works
Self-citationLewis, C., Škovierová, H., Rowley, G., Řežuchová, B., Homerová, D., Stevenson, A. W., Sherry, A., Kormanec, J., & Roberts, M. (2008) · Microbiology · doi:10.1099/mic.0.2007/011999-0 · Cited by 35 · see citing works
Self-citationYamamoto, T., Hanawa, T., Ogata, S., & Kamiya, S. (1997) · Infection and Immunity · doi:10.1128/iai.65.6.2190-2196.1997 · Cited by 31 · see citing works
Effect of Inactivation of degS on Salmonella enterica Serovar Typhimurium In Vitro and In Vivo
Rowley, G., Stevenson, A. W., Kormanec, J., & Roberts, M. (2004) · Infection and Immunity · doi:10.1128/iai.73.1.459-463.2005 · Cited by 31 · see citing works
Self-citationResto-Ruiz, S. I., Sweger, D., Widen, R. H., Valkov, N. I., & ANDERSON, B. E. (2000) · Infection and Immunity · doi:10.1128/iai.68.10.5970-5978.2000 · Cited by 28 · see citing works
Characterisation of the S. Typhimurium σE regulon
Rowley, G. (2005) · Enlighten: Theses (The University of Glasgow) · Cited by 1 · see citing works
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Spector, M. P., & Kenyon, W. J. (2011) · Food Research International · doi:10.1016/j.foodres.2011.06.056 · Cited by 268 · see citing works
Proteases in bacterial pathogenesis
Ingmer, H., & Brøndsted, L. (2009) · Research in Microbiology · doi:10.1016/j.resmic.2009.08.017 · Cited by 172 · see citing works
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Frees, D., Brøndsted, L., & Ingmer, H. (2013) · Subcellular Biochemistry · doi:10.1007/978-94-007-5940-4_7 · Cited by 159 · see citing works
Bacterial proteolytic complexes as therapeutic targets
Raju, R. M., Goldberg, A. L., & Rubin, E. J. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3846 · Cited by 105 · see citing works
The delicate balance in genetically engineering live vaccines
Galen, J. E., & Curtiss, R. (2013) · Vaccine · doi:10.1016/j.vaccine.2013.12.026 · Cited by 102 · see citing works
The emerging roles of bacterial proteases in intestinal diseases
Caminero, A., Guzman, M., Libertucci, J., & Lomax, A. E. (2023) · Gut Microbes · doi:10.1080/19490976.2023.2181922 · Cited by 92 · see citing works
Heimesaat, M. M., Alutis, M. E., Grundmann, U., Fischer, A., Tegtmeyer, N., Böhm, M., Kühl, A. A., Göbel, U. B., Backert, S., & Bereswill, S. (2014) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2014.00077 · Cited by 92 · see citing works
Effect of sublethal heat stress on Salmonella Typhimurium virulence
Sirsat, S. A., Burkholder, K. M., Muthaiyan, A., Dowd, S. E., Bhunia, A. K., & Ricke, S. C. (2011) · Journal of Applied Microbiology · doi:10.1111/j.1365-2672.2011.04941.x · Cited by 82 · see citing works
Temperature-driven differential gene expression by RNA thermosensors
Krajewski, S. S., & Narberhaus, F. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.03.006 · Cited by 66 · see citing works
Sawa-Makarska, J. Z., Malet, H., Krojer, T. J., Canellas, F., Ehrmann, M., & Clausen, T. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.243832 · Cited by 62 · see citing works
Bæk, K. T., Vegge, C. S., Skórko‐Glonek, J., & Brøndsted, L. (2010) · Applied and Environmental Microbiology · doi:10.1128/aem.01603-10 · Cited by 58 · see citing works
The Potential Link between Thermal Resistance and Virulence in Salmonella: A Review
Dawoud, T. M. S., Davis, M. L., Park, S. H., Kim, S. A., Kwon, Y. M., Jarvis, N. A., O’Bryan, C. A., Shi, Z., Crandall, P. G., & Ricke, S. C. (2017) · Frontiers in Veterinary Science · doi:10.3389/fvets.2017.00093 · Cited by 56 · see citing works
HtrA chaperone activity contributes to host cell binding in Campylobacter jejuni
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Klinkert, B., Cimdins, A., Gaubig, L. C., Roßmanith, J., Aschke-Sonnenborn, U., & Narberhaus, F. (2012) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2012.01.007 · Cited by 42 · see citing works
Ye, M., Sharma, K., Thakur, M., Smith, A. A., Büyüktanır, Ö., Xiang, X., Yang, X., Promnares, K., Lou, Y., Yang, X. F., et al. (2016) · Infection and Immunity · doi:10.1128/iai.00360-16 · Cited by 41 · see citing works
Subramaniam, S., Müller, V. S., Hering, N. A., Mollenkopf, H., Becker, D., Heroven, A. K., Dersch, P., Pohlmann, A., Tedin, K., Porwollik, S., et al. (2019) · PLoS ONE · doi:10.1371/journal.pone.0211584 · Cited by 32 · see citing works
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Runkel, S., Wells, H. C., & Rowley, G. (2013) · Advances in applied microbiology · doi:10.1016/b978-0-12-407678-5.00003-9 · Cited by 27 · see citing works
Self-citationSamazan, F., Rokbi, B., Seguin, D., Telles, F., Gautier, V., Richarme, G., Chevret, D., Varela, P. F., Velours, C., & Poquet, I. (2015) · Microbial Cell Factories · doi:10.1186/s12934-015-0271-z · Cited by 24 · see citing works
Jitprasutwit, S., Ong, C., Juntawieng, N., Ooi, W. F., Hemsley, C. M., Vattanaviboon, P., Titball, R. W., Tan, P. B. O., & Korbsrisate, S. (2014) · BMC Genomics · doi:10.1186/1471-2164-15-787 · Cited by 22 · see citing works
Raspoet, R., Shearer, N., Appia‐Ayme, C., Haesebrouck, F., Ducatelle, R., Thompson, A., & Immerseel, F. V. (2014) · Poultry Science · doi:10.3382/ps.2013-03711 · Cited by 21 · see citing works
Israeli, M., Elia, U., Rotem, S., Cohen, H., Tidhar, A., Bercovich-Kinori, A., Cohen, O., & Chitlaru, T. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.00255 · Cited by 20 · see citing works
Rowley, G., Škovierová, H., Stevenson, A. W., Řežuchová, B., Homerová, D., Lewis, C., Sherry, A., Kormanec, J., & Roberts, M. (2010) · Microbiology · doi:10.1099/mic.0.046011-0 · Cited by 19 · see citing works
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Arunima, A., Swain, S. K., Ray, S., Prusty, B. K., & Suar, M. (2020) · Virulence · doi:10.1080/21505594.2020.1743540 · Cited by 16 · see citing works
Lee, J. J., Simborio, H. L. T., Reyes, A. W. B., Kim, D.-G., Hop, H. T., Min, W., Her, M., Jung, S. C., Yoo, H. S., & Kim, S. (2014) · FEMS Microbiology Letters · doi:10.1111/1574-6968.12522 · Cited by 14 · see citing works
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Yu, B., Yang, M., Wong, H. Y. B., Watt, R. M., Song, E., Zheng, B., Yuen, K., & Huang, J.-D. (2011) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-011-3317-0 · Cited by 14 · see citing works
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Zhu, C., Xiong, K., Chen, Z., Hu, X., Li, J., Wang, Y., Rao, X., & Cong, Y. (2015) · Microbiology and Immunology · doi:10.1111/1348-0421.12276 · Cited by 13 · see citing works
Huston, W. M. (2010) · FEMS Immunology & Medical Microbiology · doi:10.1111/j.1574-695x.2010.00672.x · Cited by 12 · see citing works
Marsh, J. W., Lott, W. B., Tyndall, J. D. A., & Huston, W. M. (2013) · Cellular & Molecular Biology Letters · doi:10.2478/s11658-013-0103-2 · Cited by 12 · see citing works
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Koper, T., Polit, A., Sobiecka-Szkatuła, A., Wegrzyn, K. E., Scirè, A., Figaj, D., Kadziński, L., Zarzecka, U., Żurawa‐Janicka, D., Banecki, B., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0117413 · Cited by 11 · see citing works
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Fuche, F. J., Jones, J. A., Ramachandran, G., Higginson, E. E., Simon, R., & Tennant, S. M. (2018) · Human Vaccines & Immunotherapeutics · doi:10.1080/21645515.2018.1491499 · Cited by 11 · see citing works
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Wang, L., Ji, C., Xia, X., Cai, X., Meng, Q., & Qiao, J. (2022) · Pathogens · doi:10.3390/pathogens11101137 · Cited by 10 · see citing works
Dutta, A., Katarkar, A., & Chaudhuri, K. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056725 · Cited by 10 · see citing works
Kenyon, W. J., Humphreys, S., Roberts, M., & Spector, M. P. (2010) · Antonie van Leeuwenhoek · doi:10.1007/s10482-010-9428-2 · Cited by 10 · see citing works
Self-citationHews, C. L., Pritchard, E. J., & Rowley, G. (2019) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2019.00263 · Cited by 9 · see citing works
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Folorunso, O. S., Adeola, S., & Giwa-Ajeniya, A. O. (2020) · Pakistan Journal of Biological Sciences · doi:10.3923/pjbs.2020.628.637 · Cited by 4 · see citing works
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Lo, H., Chang, H., Wu, Y., Liao, C., & Hsiao, Y. (2024) · Journal of Basic Microbiology · doi:10.1002/jobm.202300441 · Cited by 2 · see citing works
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Yong, A. M. H., Colomer‐Winter, C., Chong, K. K. L., Gao, I. H., Matysik, A. S., Chen, S. L., & Kline, K. A. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.11.20.567783 · Cited by 1 · see citing works
Antimicrobial Effectors Act Cooperatively to Stress Salmonella in the Macrophage Phagosome
Kim, B. (2011) · Illinois Digital Environment for Access to Learning and Scholarship (University of Illinois at Urbana-Champaign)
Gain-of-function study reveals the pleiotropic roles of serine protease HtrA in Borrelia burgdorferiPreprint
Zhang, K., Sze, C. W., Zhao, H., Liu, J., & Li, C. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.08.28.610130
Distinct modes of redox-mediated DegP activation govern its role as a general proteasePreprint
Roy, D., Nandakumar, A., & Chaba, R. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.11.03.686187
- Authors
- Lewis, C., Skovierova, H., Rowley, G., Rezuchova, B., Homerova, D., Stevenson, A., Spencer, J., Farn, J., Kormanec, J., & Roberts, M.
- Affiliations
- University of Glasgow (GB)
- Institute of Molecular Biology, Slovak Academy of Science, Dubravska cesta 21, 845 51 Bratislava, Slovak Republik
- University of East Anglia (GB)
- Venue
- Microbiology
- Publisher
- Microbiology Society
- Published
- 2009-03-01
- Volume
- 155
- Issue
- 3
- Pages
- 873-881
- ISSN
- 1350-0872 (ISSN-L)
- 1465-2080
- OpenAlex
- W2118603057
- Cited by
- 54
- References
- 45
- Citations by year
- 2025: 1 · 2024: 3 · 2023: 2 · 2022: 2 · 2020: 2 · 2019: 7 · 2018: 1 · 2017: 2 · 2016: 2 · 2015: 4 · 2014: 5 · 2013: 6 · 2012: 2
- FWCI
- 2.28
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Microbiology (publishedVersion)
- PubMed (publishedVersion)
- ResearchOnline (acceptedVersion)
- ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (submittedVersion)
- ResearchOnline (Glasgow Caledonian University) (submittedVersion)
- UEA Digital Repository (University of East Anglia) (submittedVersion)
- Funders
- Wellcome Trust (065027)
- Slovenská Akadémia Vied
- Vedecká Grantová Agentúra MŠVVaŠ SR a SAV
- Biotechnology and Biological Sciences Research Council (PRS12222)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Agricultural and Biological Sciences › Food Science › Salmonella and Campylobacter epidemiology
- Keywords
- HtrA, chaperone activity, proteolytic activity, sigma E, RpoE, sigma70, promoter analysis, gene expression regulation, intramacrophage survival, bacterial virulence, heat shock, protein degradation, mouse infection, attenuated strains
- MeSH terms
- Animals, Bacterial Proteins, Base Sequence, Escherichia coli, Female, Genes, Bacterial, Genetic Complementation Test, Mice, Inbred BALB C, Molecular Sequence Data, Peptide Hydrolases, Promoter Regions, Genetic, RNA, Bacterial, Salmonella Infections, Salmonella typhimurium, Sigma Factor, Gene Expression Regulation, Bacterial, Point Mutation, Sequence Deletion, Molecular Chaperones, Mice
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