Thermal control of virulence factors in bacteria: A hot topic

References

• Marteyn B, West NP, Browning DF, Cole JA, Shaw JG, Palm F, Mounier J, Prévost M-C, Sansonetti P, Tang CM. Modulation of Shigella virulence in response to available oxygen in vivo. Nature 2010; 465:355-8; PMID:20436458; http://dx.doi.org/10.1038/nature08970
   PubMed Web of Science ®Google Scholar
• Smirnova A V, Wang L, Rohde B, Budde I, Weingart H, Ullrich MS. Control of temperature-responsive synthesis of the phytotoxin coronatine in Pseudomonas syringae by the unconventional two-component system CorRPS. J Mol Microbiol Biotechnol 2002; 4:191-6; PMID:11931546.
   PubMed Web of Science ®Google Scholar
• Starke M, Fuchs TM. YmoA negatively controls the expression of insecticidal genes in Yersinia enterocolitica. Mol Microbiol 2014; 92:287-301; PMID:24548183; http://dx.doi.org/10.1111/mmi.12554
   PubMedGoogle Scholar
• Starke M, Richter M, Fuchs TM. The insecticidal toxin genes of Yersinia enterocolitica are activated by the thermolabile LTTR-like regulator TcaR2 at low temperatures. Mol Microbiol 2013; 89:596-611; PMID:23772992; http://dx.doi.org/10.1111/mmi.12296
   PubMedGoogle Scholar
• Ye F, Brauer T, Niehus E, Drlica K, Josenhans C, Suerbaum S. Flagellar and global gene regulation in Helicobacter pylori modulated by changes in DNA supercoiling. Int J Med Microbiol 2007; 297:65-81; PMID:17276136; http://dx.doi.org/10.1016/j.ijmm.2006.11.006
   PubMedGoogle Scholar
• Eriksson S, Hurme R, Rhen M. Low-temperature sensors in bacteria. Philos Trans R Soc Lond B Biol Sci 2002; 357:887-93; PMID:12171652; http://dx.doi.org/10.1098/rstb.2002.1077
   PubMed Web of Science ®Google Scholar
• Kelly A, Conway C, O Cróinín T, Smith SGJ, Dorman CJ. DNA supercoiling and the Lrp protein determine the directionality of fim switch DNA inversion in Escherichia coli K-12. J Bacteriol 2006; 188:5356-63; PMID:16855224; http://dx.doi.org/10.1128/JB.00344-06
   PubMed Web of Science ®Google Scholar
• O Cróinín T, Carroll RK, Kelly A, Dorman CJ. Roles for DNA supercoiling and the Fis protein in modulating expression of virulence genes during intracellular growth of Salmonella enterica serovar Typhimurium. Mol Microbiol 2006; 62:869-82; http://dx.doi.org/10.1111/j.1365-2958.2006.05416.x
   PubMed Web of Science ®Google Scholar
• Prosseda G, Falconi M, Giangrossi M, Gualerzi CO, Micheli G, Colonna B. The virF promoter in Shigella: more than just a curved DNA stretch. Mol Microbiol 2004; 51:523-37; PMID:14756791; http://dx.doi.org/10.1046/j.1365-2958.2003.03848.x
   PubMed Web of Science ®Google Scholar
• Tendeng C, Bertin PN. H-NS in Gram-negative bacteria: a family of multifaceted proteins. Trends Microbiol 2003; 11:511-8; PMID:14607068; http://dx.doi.org/10.1016/j.tim.2003.09.005
   PubMedGoogle Scholar
• Tobe T, Yoshikawa M, Mizuno T, Sasakawa C. Transcriptional control of the invasion regulatory gene virB of Shigella flexneri: activation by virF and repression by H-NS. J Bacteriol 1993; 175:6142-9; PMID:7691791.
   PubMed Web of Science ®Google Scholar
• Müller CM, Dobrindt U, Nagy G, Emödy L, Uhlin BE, Hacker J. Role of histone-like proteins H-NS and StpA in expression of virulence determinants of uropathogenic Escherichia coli. J Bacteriol 2006; 188:5428-38; PMID:16855232; http://dx.doi.org/10.1128/JB.01956-05
   PubMed Web of Science ®Google Scholar
• Nye MB, Pfau JD, Skorupski K, Taylor RK. Vibrio cholerae H-NS silences virulence gene expression at multiple steps in the ToxR regulatory cascade. J Bacteriol 2000; 182:4295-303; PMID:10894740; http://dx.doi.org/10.1128/JB.182.15.4295-4303.2000
   PubMedGoogle Scholar
• Mühldorfer I, Hacker J, Keusch GT, Acheson DW, Tschäpe H, Kane A V, Ritter A, Olschläger T, Donohue-Rolfe A. Regulation of the Shiga-like toxin II operon in Escherichia coli. Infect Immun 1996; 64:495-502; PMID:8550198.
   PubMed Web of Science ®Google Scholar
• Dame RT, Wyman C, Goosen N. Structural basis for preferential binding of H-NS to curved DNA. Biochimie 2001; 83:231-4; PMID:11278073; http://dx.doi.org/10.1016/S0300-9084(00)01213-X
   PubMed Web of Science ®Google Scholar
• Dame RT, Wyman C, Wurm R, Wagner R, Goosen N. Structural basis for H-NS-mediated trapping of RNA polymerase in the open initiation complex at the rrnB P1. J Biol Chem 2002; 277:2146-50; PMID:11714691; http://dx.doi.org/10.1074/jbc.C100603200
   PubMed Web of Science ®Google Scholar
• Stella S, Falconi M, Lammi M, Gualerzi CO, Pon CL. Environmental control of the in vivo oligomerization of nucleoid protein H-NS. J Mol Biol 2006; 355:169-74; PMID:16303134; http://dx.doi.org/10.1016/j.jmb.2005.10.034
   PubMedGoogle Scholar
• Ono S, Goldberg MD, Olsson T, Esposito D, Hinton JCD, Ladbury JE. H-NS is a part of a thermally controlled mechanism for bacterial gene regulation. Biochem J 2005; 391:203-13.; .
   Google Scholar
• Akbar S, Schechter LM, Lostroh CP, Lee CA. AraC/XylS family members, HilD and HilC, directly activate virulence gene expression independently of HilA in Salmonella typhimurium. Mol Microbiol 2003; 47:715-28; PMID:12535071; http://dx.doi.org/10.1046/j.1365-2958.2003.03322.x
   PubMedGoogle Scholar
• Madrid C, Nieto JM, Paytubi S, Falconi M, Gualerzi CO, Juárez A. Temperature- and H-NS-dependent regulation of a plasmid-encoded virulence operon expressing Escherichia coli hemolysin. J Bacteriol 2002; 184:5058-66; PMID:12193622; http://dx.doi.org/10.1128/JB.184.18.5058-5066.2002
   PubMedGoogle Scholar
• Johansson J. RNA thermosensors in bacterial pathogens. Contrib Microbiol 2009; 16:150-60; PMID:19494584; http://dx.doi.org/10.1159/000219378
   PubMedGoogle Scholar
• Kortmann J, Narberhaus F. Bacterial RNA thermometers: molecular zippers and switches. Nat Rev Microbiol 2012; 10:255-65; PMID:22421878; http://dx.doi.org/10.1038/nrmicro2730
   PubMed Web of Science ®Google Scholar
• Chowdhury S, Maris C, Allain FH-T, Narberhaus F. Molecular basis for temperature sensing by an RNA thermometer. EMBO J 2006; 25:2487-97; PMID:16710302; http://dx.doi.org/10.1038/sj.emboj.7601128
   PubMedGoogle Scholar
• Waldminghaus T, Heidrich N, Brantl S, Narberhaus F. FourU: a novel type of RNA thermometer in Salmonella. Mol Microbiol 2007; 65:413-24; PMID:17630972; http://dx.doi.org/10.1111/j.1365-2958.2007.05794.x
   PubMed Web of Science ®Google Scholar
• Kortmann J, Sczodrok S, Rinnenthal J, Schwalbe H, Narberhaus F. Translation on demand by a simple RNA-based thermosensor. Nucleic Acids Res 2011; 39:2855-68; PMID:21131278; http://dx.doi.org/10.1093/nar/gkq1252
   PubMed Web of Science ®Google Scholar
• Loh E, Memarpour F, Vaitkevicius K, Kallipolitis BH, Johansson J, Sondén B. An unstructured 5’-coding region of the prfA mRNA is required for efficient translation. Nucleic Acids Res 2012; 40:1818-27; PMID:22053088; http://dx.doi.org/10.1093/nar/gkr850
   PubMedGoogle Scholar
• Giuliodori AM, Di Pietro F, Marzi S, Masquida B, Wagner R, Romby P, Gualerzi CO, Pon CL. The cspA mRNA is a thermosensor that modulates translation of the cold-shock protein CspA. Mol Cell 2010; 37:21-33; PMID:20129052; http://dx.doi.org/10.1016/j.molcel.2009.11.033
   PubMed Web of Science ®Google Scholar
• Mao Y, Najafabadi HS, Salavati R. Genome-wide computational identification of functional RNA elements in Trypanosoma brucei. BMC Genomics 2009; 10:355; PMID:19653906; http://dx.doi.org/10.1186/1471-2164-10-355
   PubMedGoogle Scholar
• Rabani M, Kertesz M, Segal E. Computational prediction of RNA structural motifs involved in posttranscriptional regulatory processes. Proc Natl Acad Sci U S A 2008; 105:14885-90; PMID:18815376; http://dx.doi.org/10.1073/pnas.0803169105
   PubMed Web of Science ®Google Scholar
• Loh E, Dussurget O, Gripenland J, Vaitkevicius K, Tiensuu T, Mandin P, Repoila F, Buchrieser C, Cossart P, Johansson J. A trans-acting riboswitch controls expression of the virulence regulator PrfA in Listeria monocytogenes. Cell 2009; 139:770-9; PMID:19914169; http://dx.doi.org/10.1016/j.cell.2009.08.046
   PubMed Web of Science ®Google Scholar
• Waters LSS. Regulatory RNAs in Bacteria. Cell 2009; 136:615-28; PMID:19239884; http://dx.doi.org/10.1016/j.cell.2009.01.043
   PubMed Web of Science ®Google Scholar
• Laalami S, Zig L, Putzer H. Initiation of mRNA decay in bacteria. Cell Mol Life Sci 2014; 71:1799-828; PMID:24064983; http://dx.doi.org/10.1007/s00018-013-1472-4
   PubMed Web of Science ®Google Scholar
• Gripenland J, Netterling S, Loh E, Tiensuu T, Toledo-Arana A, Johansson J. RNAs: regulators of bacterial virulence. Nat Rev Microbiol 2010; 8:857-66; PMID:21079634; http://dx.doi.org/10.1038/nrmicro2457
   PubMed Web of Science ®Google Scholar
• Schuck A, Diwa A, Belasco JG. RNase E autoregulates its synthesis in Escherichia coli by binding directly to a stem-loop in the rne 5’ untranslated region. Mol Microbiol 2009; 72:470-8; PMID:19320830; http://dx.doi.org/10.1111/j.1365-2958.2009.06662.x
   PubMed Web of Science ®Google Scholar
• Caron M-P, Lafontaine DA, Massé E. Small RNA-mediated regulation at the level of transcript stability. RNA Biol 7:140-4; PMID:20220305; http://dx.doi.org/10.4161/rna.7.2.11056
   PubMed Web of Science ®Google Scholar
• Pichon C, du Merle L, Lequeutre I, Le Bouguénec C. The AfaR small RNA controls expression of the AfaD-VIII invasin in pathogenic Escherichia coli strains. Nucleic Acids Res 2013; 41:5469-82; PMID:23563153; http://dx.doi.org/10.1093/nar/gkt208
   PubMed Web of Science ®Google Scholar
• Beauregard A, Smith EA, Petrone BL, Singh N, Karch C, McDonough KA, Wade JT. Identification and characterization of small RNAs in Yersinia pestis. RNA Biol 2013; 10:397-405; PMID:23324607; http://dx.doi.org/10.4161/rna.23590
   PubMed Web of Science ®Google Scholar
• Mitobe J, Morita-Ishihara T, Ishihama A, Watanabe H. Involvement of RNA-binding protein Hfq in the post-transcriptional regulation of invE gene expression in Shigella sonnei. J Biol Chem 2008; 283:5738-47; PMID:18156173; http://dx.doi.org/10.1074/jbc.M710108200
   PubMedGoogle Scholar
• Vogel J, Luisi BF. Hfq and its constellation of RNA. Nat Rev Microbiol 2011; 9:578-89; PMID:21760622; http://dx.doi.org/10.1038/nrmicro2615
   PubMed Web of Science ®Google Scholar
• Chao Y, Vogel J. The role of Hfq in bacterial pathogens. Curr Opin Microbiol 2010; 13:24-33; PMID:20080057; http://dx.doi.org/10.1016/j.mib.2010.01.001
   PubMed Web of Science ®Google Scholar
• Fantappiè L, Metruccio MME, Seib KL, Oriente F, Cartocci E, Ferlicca F, Giuliani MM, Scarlato V, Delany I. The RNA chaperone Hfq is involved in stress response and virulence in Neisseria meningitidis and is a pleiotropic regulator of protein expression. Infect Immun 2009; 77:1842-53; http://dx.doi.org/10.1128/IAI.01216-08
   PubMed Web of Science ®Google Scholar
• Quade N, Mendonca C, Herbst K, Heroven AK, Ritter C, Heinz DW, Dersch P. Structural basis for intrinsic thermosensing by the master virulence regulator RovA of Yersinia. J Biol Chem 2012; 287:35796-803; PMID:22936808; http://dx.doi.org/10.1074/jbc.M112.379156
   PubMed Web of Science ®Google Scholar
• Kamp HD, Higgins DE. A protein thermometer controls temperature-dependent transcription of flagellar motility genes in Listeria monocytogenes. PLoS Pathog 2011; 7:e1002153; PMID:21829361; http://dx.doi.org/10.1371/journal.ppat.1002153
   PubMedGoogle Scholar
• Rothenbacher FP, Zhu J. Efficient responses to host and bacterial signals during Vibrio cholerae colonization. Gut Microbes 5:120-8; PMID:24256715; http://dx.doi.org/10.4161/gmic.26944
   PubMedGoogle Scholar
• Johansson J, Mandin P, Renzoni A. An RNA Thermosensor Controls Expression of Virulence Genes in Listeria monocytogenes. Cell 2002; 110:551-61; PMID:12230973; http://dx.doi.org/10.1016/S0092-8674(02)00905-4
   PubMed Web of Science ®Google Scholar
• Marceau M. Transcriptional regulation in Yersinia: an update. Curr Issues Mol Biol 2005; 7:151-77; PMID:16053248.
   PubMed Web of Science ®Google Scholar
• Han Y, Zhou D, Pang X, Song Y, Zhang L, Bao J, Tong Z, Wang J, Guo Z, Zhai J, et al. Microarray analysis of temperature-induced transcriptome of Yersinia pestis. Microbiol Immunol 2004; 48:791-805; PMID:15557737; http://dx.doi.org/10.1111/j.1348-0421.2004.tb03605.x
   PubMedGoogle Scholar
• Böhme K, Steinmann R, Kortmann J, Seekircher S, Heroven AK, Berger E, Pisano F, Thiermann T, Wolf-Watz H, Narberhaus F, et al. Concerted Actions of a Thermo-labile Regulator and a Unique Intergenic RNA Thermosensor Control Yersinia Virulence. PLoS Pathog 2012; 8:e1002518; PMID:22359501; http://dx.doi.org/10.1371/journal.ppat.1002518
   PubMed Web of Science ®Google Scholar
• Grosdent N, Maridonneau-Parini I, Sory M-P, Cornelis GR. Role of Yops and adhesins in resistance of Yersinia enterocolitica to phagocytosis. Infect Immun 2002; 70:4165-76; PMID:12117925; http://dx.doi.org/10.1128/IAI.70.8.4165-4176.2002
   PubMedGoogle Scholar
• Cathelyn JS, Ellison DW, Hinchliffe SJ, Wren BW, Miller VL. The RovA regulons of Yersinia enterocolitica and Yersinia pestis are distinct: evidence that many RovA-regulated genes were acquired more recently than the core genome. Mol Microbiol 2007; 66:189-205; PMID:17784909; http://dx.doi.org/10.1111/j.1365-2958.2007.05907.x
   PubMed Web of Science ®Google Scholar
• Wagner NJ, Lin CP, Borst LB, Miller VL. YaxAB, a Yersinia enterocolitica pore-forming toxin regulated by RovA. Infect Immun 2013; 81:4208-19; PMID:24002058; http://dx.doi.org/10.1128/IAI.00781-13
   PubMedGoogle Scholar
• Nagel G, Lahrz A, Dersch P. Environmental control of invasin expression in Yersinia pseudotuberculosis is mediated by regulation of RovA, a transcriptional activator of the SlyA/Hor family. Mol Microbiol 2001; 41:1249-69; PMID:11580832; http://dx.doi.org/10.1046/j.1365-2958.2001.02522.x
   PubMed Web of Science ®Google Scholar
• Cathelyn JS, Crosby SD, Lathem WW, Goldman WE, Miller VL. RovA, a global regulator of Yersinia pestis, specifically required for bubonic plague. Proc Natl Acad Sci U S A 2006; 103:13514-9; PMID:16938880; http://dx.doi.org/10.1073/pnas.0603456103
   PubMed Web of Science ®Google Scholar
• Heroven AK, Böhme K, Tran-Winkler H, Dersch P. Regulatory elements implicated in the environmental control of invasin expression in enteropathogenic Yersinia. Adv Exp Med Biol 2007; 603:156-66; PMID:17966412; http://dx.doi.org/10.1007/978-0-387-72124-8_13
   PubMedGoogle Scholar
• Herbst K, Bujara M, Heroven AK, Opitz W, Weichert M, Zimmermann A, Dersch P. Intrinsic thermal sensing controls proteolysis of Yersinia virulence regulator RovA. PLoS Pathog 2009; 5:e1000435; PMID:19468295; http://dx.doi.org/10.1371/journal.ppat.1000435
   PubMed Web of Science ®Google Scholar
• Capra EJ, Laub MT. Evolution of two-component signal transduction systems. Annu Rev Microbiol 2012; 66:325-47; PMID:22746333; http://dx.doi.org/10.1146/annurev-micro-092611-150039
   PubMed Web of Science ®Google Scholar
• Scarlato V, Aricò B, Prugnola A, Rappuoli R. Sequential activation and environmental regulation of virulence genes in Bordetella pertussis. EMBO J 1991; 10:3971-5; PMID:1718746.
   PubMed Web of Science ®Google Scholar
• Mishra M, Parise G, Jackson KD, Wozniak DJ, Deora R. The BvgAS signal transduction system regulates biofilm development in Bordetella. J Bacteriol 2005; 187:1474-84; PMID:15687212; http://dx.doi.org/10.1128/JB.187.4.1474-1484.2005
   PubMedGoogle Scholar
• Manetti R, Aricò B, Rappuoli R, Scarlato V. Mutations in the linker region of BvgS abolish response to environmental signals for the regulation of the virulence factors in Bordetella pertussis. Gene 1994; 150:123-7; PMID:7959037; http://dx.doi.org/10.1016/0378-1119(94)90870-2
   PubMed Web of Science ®Google Scholar
• Ingmer H, Brøndsted L. Proteases in bacterial pathogenesis. Res Microbiol 2009; 160:704-10; PMID:19778606; http://dx.doi.org/10.1016/j.resmic.2009.08.017
   PubMedGoogle Scholar
• Gophna U, Ron EZ. Virulence and the heat shock response. Int J Med Microbiol 2003; 292:453-61; PMID:12635928; http://dx.doi.org/10.1078/1438-4221-00230
   PubMed Web of Science ®Google Scholar
• Guisbert E, Yura T, Rhodius V a, Gross C a. Convergence of molecular, modeling, and systems approaches for an understanding of the Escherichia coli heat shock response. Microbiol Mol Biol Rev 2008; 72:545-54; PMID:18772288; http://dx.doi.org/10.1128/MMBR.00007-08
   PubMed Web of Science ®Google Scholar
• Nakahigashi K, Yanagi H, Yura T. Isolation and sequence analysis of rpoH genes encoding sigma 32 homologs from gram negative bacteria: conserved mRNA and protein segments for heat shock regulation. Nucleic Acids Res 1995; 23:4383-90; PMID:7501460.
   PubMed Web of Science ®Google Scholar
• Morita MT, Tanaka Y, Kodama TS, Kyogoku Y, Yanagi H, Yura T. Translational induction of heat shock transcription factor sigma32: evidence for a built-in RNA thermosensor. Genes Dev 1999; 13:655-65; PMID:10090722; http://dx.doi.org/10.1101/gad.13.6.655
   PubMed Web of Science ®Google Scholar
• Guisbert E, Herman C, Lu CZ, Gross C a. A chaperone network controls the heat shock response in E. coli. Genes Dev 2004; 18:2812-21; PMID:15545634; http://dx.doi.org/10.1101/gad.1219204
   PubMedGoogle Scholar
• Herman C, Thévenet D, D’Ari R, Bouloc P. Degradation of sigma 32, the heat shock regulator in Escherichia coli, is governed by HflB. Proc Natl Acad Sci U S A 1995; 92:3516-20; PMID:7724592; http://dx.doi.org/10.1073/pnas.92.8.3516
   PubMedGoogle Scholar
• Parsot C, Mekalanos JJ. Expression of ToxR, the transcriptional activator of the virulence factors in Vibrio cholerae, is modulated by the heat shock response. Proc Natl Acad Sci U S A 1990; 87:9898-902; PMID:2124707; http://dx.doi.org/10.1073/pnas.87.24.9898
   PubMed Web of Science ®Google Scholar
• Dobrindt U, Hacker J. Regulation of tRNA5Leu-encoding gene leuX that is associated with a pathogenicity island in the uropathogenic Escherichia coli strain 536. Mol Genet Genomics 2001; 265:895-904; PMID:11523807; http://dx.doi.org/10.1007/s004380100486
   PubMedGoogle Scholar
• Dobrindt U, Janke B, Piechaczek K, Nagy G, Ziebuhr W, Fischer G, Schierhorn A, Hecker M, Blum-Oehler G, Hacker J. Toxin genes on pathogenicity islands: impact for microbial evolution. Int J Med Microbiol 2000; 290:307-11; PMID:11111903; http://dx.doi.org/10.1016/S1438-4221(00)80028-4
   PubMedGoogle Scholar
• Hecker M, Schumann W, Völker U. Heat-shock and general stress response in Bacillus subtilis. Mol Microbiol 1996; 19:417-28; PMID:8830234; http://dx.doi.org/10.1046/j.1365-2958.1996.396932.x
   PubMed Web of Science ®Google Scholar
• Völker U, Engelmann S, Maul B, Riethdorf S, Völker A, Schmid R, Mach H, Hecker M. Analysis of the induction of general stress proteins of Bacillus subtilis. Microbiology 1994; 140:741-52; PMID:8012595; http://dx.doi.org/10.1099/00221287-140-4-741
   PubMedGoogle Scholar
• Maul B, Völker U, Riethdorf S, Engelmann S, Hecker M. sigma B-dependent regulation of gsiB in response to multiple stimuli in Bacillus subtilis. Mol Gen Genet 1995; 248:114-20; PMID:7651322; http://dx.doi.org/10.1007/BF02456620
   PubMedGoogle Scholar
• Bischoff M, Entenza JM, Giachino P. Influence of a functional sigB operon on the global regulators sar and agr in Staphylococcus aureus. J Bacteriol 2001; 183:5171-9; PMID:11489871; http://dx.doi.org/10.1128/JB.183.17.5171-5179.2001
   PubMed Web of Science ®Google Scholar
• Chan PF, Foster SJ. Role of SarA in virulence determinant production and environmental signal transduction in Staphylococcus aureus. J Bacteriol 1998; 180:6232-41; PMID:9829932.
   PubMed Web of Science ®Google Scholar
• Chastanet A, Fert J, Msadek T. Comparative genomics reveal novel heat shock regulatory mechanisms in Staphylococcus aureus and other Gram-positive bacteria. Mol Microbiol 2003; 47:1061-73; PMID:12581359; http://dx.doi.org/10.1046/j.1365-2958.2003.03355.x
   PubMedGoogle Scholar
• De Oliveira NEM, Abranches J, Gaca AO, Laport MS, Damaso CR, Bastos M do C, de F, Lemos JA, Giambiagi-deMarval M. clpB, a class III heat-shock gene regulated by CtsR, is involved in thermotolerance and virulence of Enterococcus faecalis. Microbiology 2011; 157:656-65; PMID:21148206; http://dx.doi.org/10.1099/mic.0.041897-0
   PubMed Web of Science ®Google Scholar
• Elsholz AKW, Michalik S, Zühlke D, Hecker M, Gerth U. CtsR, the Gram-positive master regulator of protein quality control, feels the heat. EMBO J 2010; 29:3621-9; PMID:20852588; http://dx.doi.org/10.1038/emboj.2010.228
   PubMedGoogle Scholar
• Farrand AJ, Reniere ML, Ingmer H, Frees D, Skaar EP. Regulation of host hemoglobin binding by the Staphylococcus aureus Clp proteolytic system. J Bacteriol 2013; 195:5041-50; PMID:23995637; http://dx.doi.org/10.1128/JB.00505-13
   PubMedGoogle Scholar
• Knudsen GM, Olsen JE, Aabo S, Barrow P, Rychlik I, Thomsen LE. ClpP deletion causes attenuation of Salmonella Typhimurium virulence through mis-regulation of RpoS and indirect control of CsrA and the SPI genes. Microbiology 2013; 159:1497-509; PMID:23676436; http://dx.doi.org/10.1099/mic.0.065797-0
   PubMedGoogle Scholar
• Meibom KL, Dubail I, Dupuis M, Barel M, Lenco J, Stulik J, Golovliov I, Sjöstedt A, Charbit A. The heat-shock protein ClpB of Francisella tularensis is involved in stress tolerance and is required for multiplication in target organs of infected mice. Mol Microbiol 2008; 67:1384-401; PMID:18284578; http://dx.doi.org/10.1111/j.1365-2958.2008.06139.x
   PubMed Web of Science ®Google Scholar
• Chastanet A, Derre I, Nair S, Msadek T. clpB, a novel member of the Listeria monocytogenes CtsR regulon, is involved in virulence but not in general stress tolerance. J Bacteriol 2004; 186:1165-74; PMID:14762012; http://dx.doi.org/10.1128/JB.186.4.1165-1174.2004
   PubMedGoogle Scholar
• Hanawa T, Fukuda M, Kawakami H, Hirano H, Kamiya S, Yamamoto T. The Listeria monocytogenes DnaK chaperone is required for stress tolerance and efficient phagocytosis with macrophages. Cell Stress Chaperones 1999; 4:118-28; PMID:10547061.
   PubMed Web of Science ®Google Scholar
• Salman H, Libchaber A. A concentration-dependent switch in the bacterial response to temperature. Nat Cell Biol 2007; 9:1098-100; PMID:17694049; http://dx.doi.org/10.1038/ncb1632
   PubMedGoogle Scholar
• Paster E, Ryu WS. The thermal impulse response of Escherichia coli. Proc Natl Acad Sci U S A 2008; 105:5373-7; PMID:18385380; http://dx.doi.org/10.1073/pnas.0709903105
   PubMed Web of Science ®Google Scholar
• Maeda K, Imae Y, Shioi JI, Oosawa F. Effect of temperature on motility and chemotaxis of Escherichia coli. J Bacteriol 1976; 127:1039-46; PMID:783127
   PubMed Web of Science ®Google Scholar
• Maeda K, Imae Y. Thermosensory transduction in Escherichia coli: inhibition of the thermoresponse by L-serine. Proc Natl Acad Sci U S A 1979; 76:91-5; PMID:370831; http://dx.doi.org/10.1073/pnas.76.1.91
   PubMedGoogle Scholar
• Wadhams GH, Armitage JP. Making sense of it all: bacterial chemotaxis. Nat Rev Mol Cell Biol 2004; 5:1024-37; PMID:15573139; http://dx.doi.org/10.1038/nrm1524
   PubMed Web of Science ®Google Scholar
• Hazelbauer GL, Falke JJ, Parkinson JS. Bacterial chemoreceptors: high-performance signaling in networked arrays. Trends Biochem Sci 2008; 33:9-19; PMID:18165013; http://dx.doi.org/10.1016/j.tibs.2007.09.014
   PubMed Web of Science ®Google Scholar
• Nara T, Kawagishi I, Nishiyama S, Homma M, Imae Y. Modulation of the thermosensing profile of the Escherichia coli aspartate receptor tar by covalent modification of its methyl-accepting sites. J Biol Chem 1996; 271:17932-6; PMID:8663384; http://dx.doi.org/10.1074/jbc.271.30.17932
   PubMedGoogle Scholar
• Tagkopoulos I, Liu Y-C, Tavazoie S. Predictive behavior within microbial genetic networks. Science 2008; 320:1313-7; PMID:18467556; http://dx.doi.org/10.1126/science.1154456
   PubMedGoogle Scholar
• Ternan NG, Jain S, Srivastava M, McMullan G. Comparative transcriptional analysis of clinically relevant heat stress response in Clostridium difficile strain 630. PLoS One 2012; 7:e42410; PMID:22860125; http://dx.doi.org/10.1371/journal.pone.0042410
   PubMedGoogle Scholar
• Xu S, Peng Z, Cui B, Wang T, Song Y, Zhang L, Wei G, Wang Y, Shen X. FliS modulates FlgM activity by acting as a non-canonical chaperone to control late flagellar gene expression, motility and biofilm formation in Yersinia pseudotuberculosis. Environ Microbiol 2014; 16:1090-104; PMID:23957589; http://dx.doi.org/10.1111/1462-2920.12222
   PubMedGoogle Scholar
• Ding L, Wang Y, Hu Y, Atkinson S, Williams P, Chen S. Functional characterization of FlgM in the regulation of flagellar synthesis and motility in Yersinia pseudotuberculosis. Microbiology 2009; 155:1890-900; PMID:19383707; http://dx.doi.org/10.1099/mic.0.026294-0
   PubMedGoogle Scholar
• Kapatral V, Olson JW, Pepe JC, Miller VL, Minnich SA. Temperature-dependent regulation of Yersinia enterocolitica Class III flagellar genes. Mol Microbiol 1996; 19:1061-71; PMID:8830263; http://dx.doi.org/10.1046/j.1365-2958.1996.452978.x
   PubMedGoogle Scholar
• Rohde JR, Fox JM, Minnich SA. Thermoregulation in Yersinia enterocolitica is coincident with changes in DNA supercoiling. Mol Microbiol 1994; 12:187-99; PMID:8057844; http://dx.doi.org/10.1111/j.1365-2958.1994.tb01008.x
   PubMedGoogle Scholar
• Guerry P, Alm RA, Power ME, Logan SM, Trust TJ. Role of two flagellin genes in Campylobacter motility. J Bacteriol 1991; 173:4757-64; PMID:1856171.
   PubMed Web of Science ®Google Scholar
• Alm RA, Guerry P, Trust TJ. The Campylobacter sigma 54 flaB flagellin promoter is subject to environmental regulation. J Bacteriol 1993; 175:4448-55; PMID:8331072.
   PubMed Web of Science ®Google Scholar
• Wösten MMSM, van Dijk L, Veenendaal AKJ, de Zoete MR, Bleumink-Pluijm NMC, van Putten JPM. Temperature-dependent FlgM/FliA complex formation regulates Campylobacter jejuni flagella length. Mol Microbiol 2010; 75:1577-91; PMID:20199595; http://dx.doi.org/10.1111/j.1365-2958.2010.07079.x
   PubMedGoogle Scholar
• Johannes L, Römer W. Shiga toxins–from cell biology to biomedical applications. Nat Rev Microbiol 2010; 8:105-16; PMID:20023663.
   PubMed Web of Science ®Google Scholar
• Mikulskis A V, Delor I, Thi VH, Cornelis GR. Regulation of the Yersinia enterocolitica enterotoxin Yst gene. Influence of growth phase, temperature, osmolarity, pH and bacterial host factors. Mol Microbiol 1994; 14:905-15; PMID:7715452; http://dx.doi.org/10.1111/j.1365-2958.1994.tb01326.x
   PubMedGoogle Scholar
• Delor I, Cornelis GR. Role of Yersinia enterocolitica Yst toxin in experimental infection of young rabbits. Infect Immun 1992; 60:4269-77; PMID:1398938.
   PubMed Web of Science ®Google Scholar
• Dai Z, Koehler TM. Regulation of anthrax toxin activator gene (atxA) expression in Bacillus anthracis: temperature, not CO2/bicarbonate, affects AtxA synthesis. Infect Immun 1997; 65:2576-82; PMID:9199422.
   PubMed Web of Science ®Google Scholar
• Dai Z, Sirard JC, Mock M, Koehler TM. The atxA gene product activates transcription of the anthrax toxin genes and is essential for virulence. Mol Microbiol 1995; 16:1171-81; PMID:8577251; http://dx.doi.org/10.1111/j.1365-2958.1995.tb02340.x
   PubMedGoogle Scholar
• Sirard JC, Mock M, Fouet A. The three Bacillus anthracis toxin genes are coordinately regulated by bicarbonate and temperature. J Bacteriol 1994; 176:5188-92; PMID:8051039.
   PubMed Web of Science ®Google Scholar
• Fouet A. AtxA, a Bacillus anthracis global virulence regulator. Res Microbiol 2010; 161:735-42; PMID:20863885; http://dx.doi.org/10.1016/j.resmic.2010.09.006
   PubMedGoogle Scholar
• Kazmierczak MJ, Wiedmann M, Boor KJ. Alternative Sigma Factors and Their Roles in Bacterial Virulence. Microbiol Mol Biol Rev 2005; 69:527-43; PMID:16339734; http://dx.doi.org/10.1128/MMBR.69.4.527-543.2005
   PubMed Web of Science ®Google Scholar
• Lybecker MC, Samuels DS. Temperature-induced regulation of RpoS by a small RNA in Borrelia burgdorferi. Mol Microbiol 2007; 64:1075-89; PMID:17501929; http://dx.doi.org/10.1111/j.1365-2958.2007.05716.x
   PubMedGoogle Scholar
• Archambault L, Linscott J, Swerdlow N, Boyland K, Riley E, Schlax P. Translational efficiency of rpoS mRNA from Borrelia burgdorferi: effects of the length and sequence of the mRNA leader region. Biochem Biophys Res Commun 2013; 433:73-8; PMID:23454119; http://dx.doi.org/10.1016/j.bbrc.2013.02.063
   PubMedGoogle Scholar
• Hämmerle H, Večerek B, Resch A, Bläsi U. Duplex formation between the sRNA DsrA and rpoS mRNA is not sufficient for efficient RpoS synthesis at low temperature. RNA Biol 2013; 10:1834-41.
   PubMed Web of Science ®Google Scholar
• Kraiczy P, Skerka C, Brade V, Zipfel PF. Further characterization of complement regulator-acquiring surface proteins of Borrelia burgdorferi. Infect Immun 2001; 69:7800-9; PMID:11705962; http://dx.doi.org/10.1128/IAI.69.12.7800-7809.2001
   PubMed Web of Science ®Google Scholar
• Von Lackum K, Miller JC, Bykowski T, Riley SP, Woodman ME, Brade V, Kraiczy P, Stevenson B, Wallich R. Borrelia burgdorferi regulates expression of complement regulator-acquiring surface protein 1 during the mammal-tick infection cycle. Infect Immun 2005; 73:7398-405; PMID:16239539; http://dx.doi.org/10.1128/IAI.73.11.7398-7405.2005
   PubMedGoogle Scholar
• Lillard JW, Bearden SW, Fetherston JD, Perry RD. The haemin storage (Hms+) phenotype of Yersinia pestis is not essential for the pathogenesis of bubonic plague in mammals. Microbiology 1999; 145(Pt 1):197-209; PMID:10206699; http://dx.doi.org/10.1099/13500872-145-1-197
   PubMedGoogle Scholar
• Hinnebusch BJ, Perry RD, Schwan TG. Role of the Yersinia pestis hemin storage (hms) locus in the transmission of plague by fleas. Science 1996; 273:367-70; PMID:8662526; http://dx.doi.org/10.1126/science.273.5273.367
   PubMedGoogle Scholar
• Perry RD, Bobrov AG, Kirillina O, Jones HA, Pedersen L, Abney J, Fetherston JD. Temperature regulation of the hemin storage (Hms+) phenotype of Yersinia pestis is posttranscriptional. J Bacteriol 2004; 186:1638-47; PMID:14996794; http://dx.doi.org/10.1128/JB.186.6.1638-1647.2004
   PubMedGoogle Scholar
• Porcheron G, Garénaux A, Proulx J, Sabri M, Dozois CM. Iron, copper, zinc, and manganese transport and regulation in pathogenic Enterobacteria: correlations between strains, site of infection and the relative importance of the different metal transport systems for virulence. Front Cell Infect Microbiol 2013; 3:90; PMID:24367764; http://dx.doi.org/10.3389/fcimb.2013.00090
   PubMedGoogle Scholar
• Kouse AB, Righetti F, Kortmann J, Narberhaus F, Murphy ER. RNA-mediated thermoregulation of iron-acquisition genes in Shigella dysenteriae and pathogenic Escherichia coli. PLoS One 2013; 8:e63781; PMID:23704938; http://dx.doi.org/10.1371/journal.pone.0063781
   PubMed Web of Science ®Google Scholar
• Viswanathan VK. Shigella takes the temperature. Gut Microbes 4:267-8; PMID:23851363; http://dx.doi.org/10.4161/gmic.25726
   PubMedGoogle Scholar
• Xiao R, Kisaalita WS. Iron acquisition from transferrin and lactoferrin by Pseudomonas aeruginosa pyoverdin. Microbiology 1997; 143(Pt 7):2509-15; PMID:9245831; http://dx.doi.org/10.1099/00221287-143-7-2509
   PubMedGoogle Scholar
• Barbier M, Damron FH, Bielecki P, Suárez-Diez M, Puchałka J, Albertí S, Dos Santos VM, Goldberg JB. From the environment to the host: re-wiring of the transcriptome of Pseudomonas aeruginosa from 22°C to 37°C. PLoS One 2014; 9:e89941; PMID:24587139; http://dx.doi.org/10.1371/journal.pone.0089941
   PubMedGoogle Scholar
• Schneider M, Exley R. Functional significance of factor H binding to Neisseria meningitidis. J Immunol 2006; 176:7566-75; PMID:16751403; http://dx.doi.org/10.4049/jimmunol.176.12.7566
   PubMed Web of Science ®Google Scholar
• Schneider MC, Prosser BE, Caesar JJE, Kugelberg E, Li S, Zhang Q, Quoraishi S, Lovett JE, Deane JE, Sim RB, et al. Neisseria meningitidis recruits factor H using protein mimicry of host carbohydrates. Nature 2009; 458:890-3; PMID:19225461; http://dx.doi.org/10.1038/nature07769
   PubMed Web of Science ®Google Scholar
• Loh E, Kugelberg E, Tracy A, Zhang Q, Gollan B, Ewles H, Chalmers R, Pelicic V, Tang CM. Temperature triggers immune evasion by Neisseria meningitidis. Nature 2013; 502:237-40; PMID:24067614; http://dx.doi.org/10.1038/nature12616
   PubMed Web of Science ®Google Scholar
• Reinés M, Llobet E, Llompart CM, Moranta D, Pérez-Gutiérrez C, Bengoechea J a. Molecular basis of Yersinia enterocolitica temperature-dependent resistance to antimicrobial peptides. J Bacteriol 2012; 194:3173-88; http://dx.doi.org/10.1128/JB.00308-12
   PubMed Web of Science ®Google Scholar
• Li Y, Powell D. LPS remodeling is an evolved survival strategy for bacteria. PNAS 2012; 109:8716-21; PMID:22586119; http://dx.doi.org/10.1073/pnas.1202908109
   PubMedGoogle Scholar
• Bengoechea JA, Zhang L, Toivanen P, Skurnik M. Regulatory network of lipopolysaccharide O-antigen biosynthesis in Yersinia enterocolitica includes cell envelope-dependent signals. Mol Microbiol 2002; 44:1045-62; PMID:12010497; http://dx.doi.org/10.1046/j.1365-2958.2002.02940.x
   PubMedGoogle Scholar
• Bartley S, Tzeng Y, Heel K. Attachment and Invasion of Neisseria meningitidis to Host Cells Is Related to Surface Hydrophobicity, Bacterial Cell Size and Capsule. PLoS One 2013; 8:e55798; PMID:23405216; http://dx.doi.org/10.1371/journal.pone.0055798
   PubMedGoogle Scholar
• Kang SO, Wright JO, Tesorero R a, Lee H, Beall B, Cho KH. Thermoregulation of capsule production by Streptococcus pyogenes. PLoS One 2012; 7:e37367; PMID:22615992; http://dx.doi.org/10.1371/journal.pone.0037367
   PubMedGoogle Scholar
• Kang SO, Caparon MG, Cho KH. Virulence gene regulation by CvfA, a putative RNase: the CvfA-enolase complex in Streptococcus pyogenes links nutritional stress, growth-phase control, and virulence gene expression. Infect Immun 2010; 78:2754-67; PMID:20385762; http://dx.doi.org/10.1128/IAI.01370-09
   PubMed Web of Science ®Google Scholar
• Sturm A, Heinemann M, Arnoldini M. The cost of virulence: retarded growth of Salmonella typhimurium cells expressing type III secretion system 1. PLoS Pathog 2011; 7:1-10; http://dx.doi.org/10.1371/journal.ppat.1002143
   Web of Science ®Google Scholar
• Rhen M, Dorman CJ. Hierarchical gene regulators adapt Salmonella enterica to its host milieus. Int J Med Microbiol 2005; 294:487-502; PMID:15790293; http://dx.doi.org/10.1016/j.ijmm.2004.11.004
   PubMedGoogle Scholar
• Coombes BK, Brown NF, Valdez Y, Brumell JH, Finlay BB. Expression and secretion of Salmonella pathogenicity island-2 virulence genes in response to acidification exhibit differential requirements of a functional type III secretion apparatus and SsaL. J Biol Chem 2004; 279:49804-15; PMID:15383528; http://dx.doi.org/10.1074/jbc.M404299200
   PubMed Web of Science ®Google Scholar
• Deiwick J, Nikolaus T, Erdogan S, Hensel M. Environmental regulation of Salmonella pathogenicity island 2 gene expression. Mol Microbiol 1999; 31:1759-73; PMID:10209748; http://dx.doi.org/10.1046/j.1365-2958.1999.01312.x
   PubMedGoogle Scholar
• Duong N, Osborne S, Bustamante VH, Tomljenovic AM, Puente JL, Coombes BK. Thermosensing coordinates a cis-regulatory module for transcriptional activation of the intracellular virulence system in Salmonella enterica serovar Typhimurium. J Biol Chem 2007; 282:34077-84; PMID:17895240; http://dx.doi.org/10.1074/jbc.M707352200
   PubMedGoogle Scholar
• Beloin C, Dorman CJ. An extended role for the nucleoid structuring protein H-NS in the virulence gene regulatory cascade of Shigella flexneri. Mol Microbiol 2003; 47:825-38; PMID:12535079; http://dx.doi.org/10.1046/j.1365-2958.2003.03347.x
   PubMedGoogle Scholar
• Watanabe H, Arakawa E, Ito K, Kato J, Nakamura A. Genetic analysis of an invasion region by use of a Tn3-lac transposon and identification of a second positive regulator gene, invE, for cell invasion of Shigella sonnei: significant homology of invE with ParB of plasmid P1. J Bacteriol 1990; 172:619-29; PMID:1688841
   PubMed Web of Science ®Google Scholar
• Choy HA. Multiple activities of LigB potentiate virulence of Leptospira interrogans: inhibition of alternative and classical pathways of complement. PLoS One 2012; 7:e41566; PMID:22911815; http://dx.doi.org/10.1371/journal.pone.0041566
   PubMedGoogle Scholar
• Choy HA, Kelley MM, Croda J, Matsunaga J, Babbitt JT, Ko AI, Picardeau M, Haake DA. The multifunctional LigB adhesin binds homeostatic proteins with potential roles in cutaneous infection by pathogenic Leptospira interrogans. PLoS One 2011; 6:e16879; PMID:21347378; http://dx.doi.org/10.1371/journal.pone.0016879
   PubMed Web of Science ®Google Scholar
• Matsunaga J, Schlax PJ, Haake DA. Role for cis-acting RNA sequences in the temperature-dependent expression of the multiadhesive lig proteins in Leptospira interrogans. J Bacteriol 2013; 195:5092-101; PMID:24013626; http://dx.doi.org/10.1128/JB.00663-13
   PubMedGoogle Scholar