Identification of the RNA-binding domain-containing protein RbpA that acts as a global regulator of the pathogenicity of Streptococcus suis serotype 2

References

• Browning DF, Butala M, Busby SJW. Bacterial transcription factors: regulation by pick “N mix”. J Mol Biol. 2019;431:4067–4077.
   PubMed Web of Science ®Google Scholar
• Gao R, Bouillet S, Stock AM. Structural basis of response regulator function. Annu Rev Microbiol. 2019;73:175–197.
   PubMed Web of Science ®Google Scholar
• Desnoyers G, Bouchard MP, Masse E. New insights into small RNA-dependent translational regulation in prokaryotes. Trends Genet. 2013;29:92–98.
   PubMed Web of Science ®Google Scholar
• Nitzan M, Rehani R, Margalit H. Integration of bacterial small RNAs in regulatory networks. Annu Rev Biophys. 2017;46:131–148.
   PubMed Web of Science ®Google Scholar
• Van Assche E, Van Puyvelde S, Vanderleyden J, et al. RNA-binding proteins involved in post-transcriptional regulation in bacteria. Front Microbiol. 2015;6:141.
   PubMed Web of Science ®Google Scholar
• Holmqvist E, Vogel J. RNA-binding proteins in bacteria. Nat Rev Microbiol. 2018;16:601–615.
   PubMed Web of Science ®Google Scholar
• Babitzke P, Lai YJ, Renda AJ, et al. Posttranscription initiation control of gene expression mediated by bacterial RNA-binding proteins. Annu Rev Microbiol. 2019;73:43–67.
   PubMed Web of Science ®Google Scholar
• Hajnsdorf E, Boni IV. Multiple activities of RNA-binding proteins S1 and Hfq. Biochimie. 2012;94:1544–1553.
   PubMed Web of Science ®Google Scholar
• Bycroft M, Hubbard TJ, Proctor M, et al. The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold. Cell. 1997;88:235–242.
   PubMed Web of Science ®Google Scholar
• Matsumoto Y, Xu Q, Miyazaki S, et al. Structure of a virulence regulatory factor CvfB reveals a novel winged helix RNA binding module. Structure. 2010;18:537–547.
   PubMed Web of Science ®Google Scholar
• Koleva RI, Austin CA, Kowaleski JM, et al. Interactions of ribosomal protein S1 with DsrA and rpoS mRNA. Biochem Biophys Res Commun. 2006;348:662–668.
   PubMed Web of Science ®Google Scholar
• Windbichler N, von Pelchrzim F, Mayer O, et al. Isolation of small RNA-binding proteins from E. coli: evidence for frequent interaction of RNAs with RNA polymerase. RNA Biol. 2008;5:30–40.
   PubMed Web of Science ®Google Scholar
• Salah P, Bisaglia M, Aliprandi P, et al. Probing the relationship between Gram-negative and Gram-positive S1 proteins by sequence analysis. Nucleic Acids Res. 2009;37:5578–5588.
   PubMed Web of Science ®Google Scholar
• Bernhardt J, Volker U, Volker A, et al. Specific and general stress proteins in Bacillus subtilis–a two-dimensional protein electrophoresis study. Microbiology. 1997;143:999–1017.
   PubMed Web of Science ®Google Scholar
• Kaan T, Homuth G, Mader U, et al. Genome-Wide transcriptional profiling of the Bacillus subtilis cold-shock response. Microbiology. 2002;148:3441–3455.
   PubMed Web of Science ®Google Scholar
• Wang X, Niu C, Sun G, et al. Ygs is a novel gene that influences biofilm formation and the general stress response of Staphylococcus epidermidis. Infect Immun. 2011;79:1007–1015.
   PubMed Web of Science ®Google Scholar
• Michaux C, Martini C, Shioya K, et al. CspR, a cold shock RNA-binding protein involved in the long-term survival and the virulence of Enterococcus faecalis. J Bacteriol. 2012;194:6900–6908.
   PubMed Web of Science ®Google Scholar
• Duval BD, Mathew A, Satola SW, et al. Altered growth, pigmentation, and antimicrobial susceptibility properties of Staphylococcus aureus due to loss of the major cold shock gene cspB. Antimicrob Agents Chemother. 2010;54:2283–2290.
   PubMed Web of Science ®Google Scholar
• Bonifait L, Veillette M, Letourneau V, et al. Detection of Streptococcus suis in bioaerosols of swine confinement buildings. Appl Environ Microbiol. 2014;80:3296–3304.
   PubMed Web of Science ®Google Scholar
• Goyette-Desjardins G, Auger JP, Xu J, et al. Streptococcus suis, an important pig pathogen and emerging zoonotic agent-an update on the worldwide distribution based on serotyping and sequence typing. Emerg Microbes Infect. 2014;3:e45.
   PubMed Web of Science ®Google Scholar
• Segura M, Calzas C, Grenier D, et al. Initial steps of the pathogenesis of the infection caused by Streptococcus suis: fighting against nonspecific defenses. FEBS Lett. 2016;590:3772–3799.
   PubMed Web of Science ®Google Scholar
• Fittipaldi N, Segura M, Grenier D, et al. Virulence factors involved in the pathogenesis of the infection caused by the swine pathogen and zoonotic agent Streptococcus suis. Future Microbiol. 2012;7:259–279.
   PubMed Web of Science ®Google Scholar
• Wu Z, Wu C, Shao J, et al. The Streptococcus suis transcriptional landscape reveals adaptation mechanisms in pig blood and cerebrospinal fluid. Rna. 2014;20:882–898.
   PubMed Web of Science ®Google Scholar
• Feng L, Zhu J, Chang H, et al. The CodY regulator is essential for virulence in Streptococcus suis serotype 2. Sci Rep. 2016;6:21241.
   PubMed Web of Science ®Google Scholar
• Xiao G, Tang H, Zhang S, et al. Streptococcus suis small RNA rss04 contributes to the induction of meningitis by regulating capsule synthesis and by inducing biofilm formation in a mouse infection model. Vet Microbiol. 2017;199:111–119.
   PubMed Web of Science ®Google Scholar
• Zheng C, Li L, Ge H, et al. Role of two-component regulatory systems in the virulence of Streptococcus suis. Microbiol Res. 2018;214:123–128.
   PubMedGoogle Scholar
• Zhu Y, Dong W, Ma J, et al. Utilization of the ComRS system for the rapid markerless deletion of chromosomal genes in Streptococcus suis. Future Microbiol. 2019;14:207–222.
   PubMed Web of Science ®Google Scholar
• Takamatsu D, Osaki M, Sekizaki T. Construction and characterization of Streptococcus suis-Escherichia coli shuttle cloning vectors. Plasmid. 2001;45:101–113.
   PubMed Web of Science ®Google Scholar
• Waterhouse A, Bertoni M, Bienert S, et al. SWISS-MODEL: homology modelling of protein structures and complexes. Nucleic Acids Res. 2018;46:W296–w303.
   PubMed Web of Science ®Google Scholar
• Zhang Y, Zhong X, Lu P, et al. A novel autolysin AtlASS mediates bacterial cell separation during cell division and contributes to full virulence in Streptococcus suis. Vet Microbiol. 2019;234:92–100.
   PubMed Web of Science ®Google Scholar
• Huntzinger E, Boisset S, Saveanu C, et al. Staphylococcus aureus RNAIII and the endoribonuclease III coordinately regulate spa gene expression. Embo J. 2005;24:824–835.
   PubMed Web of Science ®Google Scholar
• Aviv G, Gal-Mor O. lacZ reporter system as a tool to study virulence gene regulation in bacterial pathogens. Methods Mol Biol. 2018;1734:39–45.
   PubMedGoogle Scholar
• He X, Thornton J, Carmicle-Davis S, et al. Tex, a putative transcriptional accessory factor, is involved in pathogen fitness in Streptococcus pneumoniae. Microb Pathog. 2006;41:199–206.
   PubMed Web of Science ®Google Scholar
• Matsumoto Y, Kaito C, Morishita D, et al. Regulation of exoprotein gene expression by the Staphylococcus aureus cvfB gene. Infect Immun. 2007;75:1964–1972.
   PubMed Web of Science ®Google Scholar
• Segura M, Fittipaldi N, Calzas C, et al. Critical Streptococcus suis virulence factors: are they all really critical? Trends Microbiol. 2017;25:585–599.
   PubMed Web of Science ®Google Scholar
• Nogueira T, Springer M. Post-transcriptional control by global regulators of gene expression in bacteria. Curr Opin Microbiol. 2000;3:154–158.
   PubMed Web of Science ®Google Scholar
• Chao Y, Vogel J. The role of Hfq in bacterial pathogens. Curr Opin Microbiol. 2010;13:24–33.
   PubMed Web of Science ®Google Scholar
• Vogel J, Luisi BF. Hfq and its constellation of RNA. Nat Rev Microbiol. 2011;9:578–589.
   PubMed Web of Science ®Google Scholar
• Sun X, Zhulin I, Wartell RM. Predicted structure and phyletic distribution of the RNA-binding protein Hfq. Nucleic Acids Res. 2002;30:3662–3671.
   PubMed Web of Science ®Google Scholar
• Silva LM, Baums CG, Rehm T, et al. Virulence-associated gene profiling of Streptococcus suis isolates by PCR. Vet Microbiol. 2006;115:117–127.
   PubMed Web of Science ®Google Scholar
• Zhang A, Mu X, Chen B, et al. IgA1 protease contributes to the virulence of Streptococcus suis. Vet Microbiol. 2011;148:436–439.
   PubMed Web of Science ®Google Scholar
• Telford JL, Barocchi MA, Margarit I, et al. Pili in gram-positive pathogens. Nat Rev Microbiol. 2006;4:509–519.
   PubMed Web of Science ®Google Scholar
• Fittipaldi N, Takamatsu D, de la Cruz Dominguez-Punaro M, et al. Mutations in the gene encoding the ancillary pilin subunit of the Streptococcus suis srtF cluster result in pili formed by the major subunit only. PLoS One. 2010;5:e8426.
   PubMed Web of Science ®Google Scholar
• Yu Y, Qian Y, Du D, et al. SBP2 plays an important role in the virulence changes of different artificial mutants of Streptococcus suis. Mol Biosyst. 2016;12:1948–1962.
   PubMedGoogle Scholar
• Shao J, Zhang W, Wu Z, et al. The truncated major pilin subunit Sbp2 of the srtBCD pilus cluster still contributes to Streptococcus suis pathogenesis in the absence of pilus shaft. Curr Microbiol. 2014;69:703–707.
   PubMed Web of Science ®Google Scholar
• Eckert C, Lecerf M, Dubost L, et al. Functional analysis of AtlA, the major N-acetylglucosaminidase of Enterococcus faecalis. J Bacteriol. 2006;188:8513–8519.
   PubMed Web of Science ®Google Scholar
• Bateman A, Bycroft M. The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD). J Mol Biol. 2000;299:1113–1119.
   PubMed Web of Science ®Google Scholar
• Xu B, Zhang P, Li W, et al. hsdS, belonging to the type I restriction-modification system, contributes to the Streptococcus suis serotype 2 survival ability in phagocytes. Front Microbiol. 2017;8:1524.
   PubMed Web of Science ®Google Scholar
• Görke B, Stülke J. Carbon catabolite repression in bacteria: many ways to make the most out of nutrients. Nat Rev Microbiol. 2008;6:613–624.
   PubMed Web of Science ®Google Scholar
• Zhong X, Zhang Y, Zhu Y, et al. Identification of an autorepressing two-component signaling system that modulates virulence in Streptococcus suis serotype 2. Infect Immun. 2019;87. DOI:10.1128/IAI.00377-19
   Web of Science ®Google Scholar
• Willenborg J, Fulde M, de Greeff A, et al. Role of glucose and CcpA in capsule expression and virulence of Streptococcus suis. Microbiology (Reading). 2011;157:1823–1833.
   PubMed Web of Science ®Google Scholar
• Yu W, Hu J, Yu B, et al. Solution structure of GSP13 from Bacillus subtilis exhibits an S1 domain related to cold shock proteins. J Biomol NMR. 2009;43:255–259.
   PubMed Web of Science ®Google Scholar