Staphylococcus aureus foldase PrsA contributes to the folding and secretion of protein A

Harwood CR, Cranenburgh R. Bacillus protein secretion: an unfolding story. Trends Microbiol. 2008;16(2):73–9. https://doi.org/10.1016/j.tim.2007.12.001.

Article  CAS  PubMed  Google Scholar 

Sarvas M, Harwood CR, Bron S, van Dijl JM. Post-translocational folding of secretory proteins in Gram-positive bacteria. Biochim Biophys Acta. 2004;1694(1–3):311–27. https://doi.org/10.1016/j.bbamcr.2004.04.009.

Article  CAS  PubMed  Google Scholar 

Vitikainen M, Lappalainen I, Seppala R, Antelmann H, Boer H, Taira S, et al. Structure-function analysis of PrsA reveals roles for the parvulin-like and flanking N- and C-terminal domains in protein folding and secretion in Bacillus subtilis. J Biol Chem. 2004;279(18):19302–14. https://doi.org/10.1074/jbc.M400861200.

Article  CAS  PubMed  Google Scholar 

Vitikainen M, Pummi T, Airaksinen U, Wahlstrom E, Wu H, Sarvas M, Kontinen VP. Quantitation of the capacity of the secretion apparatus and requirement for PrsA in growth and secretion of alpha-amylase in Bacillus subtilis. J Bacteriol. 2001;183(6):1881–90. https://doi.org/10.1128/JB.183.6.1881-1890.2001.

Article  CAS  PubMed  PubMed Central  Google Scholar 

Wahlstrom E, Vitikainen M, Kontinen VP, Sarvas M. The extracytoplasmic folding factor PrsA is required for protein secretion only in the presence of the cell wall in Bacillus subtilis. Microbiology. 2003;149(Pt 3):569–77. https://doi.org/10.1099/mic.0.25511-0.

Article  CAS  PubMed  Google Scholar 

Kontinen VP, Saris P, Sarvas M. A gene (prsA) of Bacillus subtilis involved in a novel, late stage of protein export. Mol Microbiol. 1991;5(5):1273–83.

Article  CAS  PubMed  Google Scholar 

Hyyrylainen HL, Marciniak BC, Dahncke K, Pietiainen M, Courtin P, Vitikainen M, et al. Penicillin-binding protein folding is dependent on the PrsA peptidyl-prolyl cis-trans isomerase in Bacillus subtilis. Mol Microbiol. 2010;77(1):108–27. https://doi.org/10.1111/j.1365-2958.2010.07188.

Article  CAS  PubMed  Google Scholar 

Williams RC, Rees ML, Jacobs MF, Pragai Z, Thwaite JE, Baillie LW, et al. Production of Bacillus anthracis protective antigen is dependent on the extracellular chaperone, PrsA. J Biol Chem. 2003;278(20):18056–62. https://doi.org/10.1074/jbc.M301244200.

Article  CAS  PubMed  Google Scholar 

Ma Y, Bryant AE, Salmi DB, Hayes-Schroer SM, McIndoo E, Aldape MJ, Stevens DL. Identification and characterization of bicistronic speB and prsA gene expression in the group a Streptococcus. J Bacteriol. 2006;188(21):7626–34. https://doi.org/10.1128/JB.01059-06.

Article  CAS  PubMed  PubMed Central  Google Scholar 

Wu ZY, Campeau A, Liu CH, Gonzalez DJ, Yamaguchi M, Kawabata S, et al. Unique virulence role of post-translocational chaperone PrsA in shaping Streptococcus pyogenes secretome. Virulence. 2021;12(1):2633–47. https://doi.org/10.1080/21505594.2021.1982501.

Article  CAS  PubMed  PubMed Central  Google Scholar 

Alonzo F 3rd, Port GC, Cao M, Freitag NE. The posttranslocation chaperone PrsA2 contributes to multiple facets of Listeria monocytogenes pathogenesis. Infect Immun. 2009;77(7):2612–23. https://doi.org/10.1128/IAI.00280-09.

Article  CAS  PubMed  PubMed Central  Google Scholar 

Zemansky J, Kline BC, Woodward JJ, Leber JH, Marquis H, Portnoy DA. Development of a mariner-based transposon and identification of Listeria monocytogenes determinants, including the peptidyl-prolyl isomerase PrsA2, that contribute to its hemolytic phenotype. J Bacteriol. 2009;191(12):3950–64. https://doi.org/10.1128/JB.00016-09.

Article  CAS  PubMed  PubMed Central  Google Scholar 

Forster BM, Zemansky J, Portnoy DA, Marquis H. Posttranslocation chaperone PrsA2 regulates the maturation and secretion of Listeria monocytogenes proprotein virulence factors. J Bacteriol. 2011;193(21):5961–70. https://doi.org/10.1128/JB.05307-11.

Article  CAS  PubMed  PubMed Central  Google Scholar 

Ahmed JK, Freitag NE. Secretion chaperones PrsA2 and HtrA are required for Listeria monocytogenes replication following intracellular induction of virulence factor secretion. Infect Immun. 2016;84(10):3034–46. https://doi.org/10.1128/IAI.00312-16.

Article  CAS  PubMed  PubMed Central  Google Scholar 

Guo L, Wu T, Hu W, He X, Sharma S, Webster P, et al. Phenotypic characterization of the foldase homologue PrsA in Streptococcus mutans. Mol Oral Microbiol. 2013;28(2):154–65. https://doi.org/10.1111/omi.12014.

Article  CAS  PubMed  Google Scholar 

Hsu CC, Hsu RB, Oon XH, Chen YT, Chen JW, Hsu CH, et al. Streptococcus mutans PrsA mediates AtlA secretion contributing to extracellular DNA release and biofilm formation in the pathogenesis of infective endocarditis. Virulence. 2022;13(1):1379–92. https://doi.org/10.1080/21505594.2022.2105351.

Article  CAS  PubMed  PubMed Central  Google Scholar 

Otto M. Staphylococcus aureus toxins. Curr Opin Microbiol. 2014;17:32–7. https://doi.org/10.1016/j.mib.2013.11.004.

Article  CAS  PubMed  Google Scholar 

Jousselin A, Renzoni A, Andrey DO, Monod A, Lew DP, Kelley WL. The posttranslocational chaperone lipoprotein PrsA is involved in both glycopeptide and oxacillin resistance in Staphylococcus aureus. Antimicrob Agents Chemother. 2012;56(7):3629–40. https://doi.org/10.1128/AAC.06264-11.

Article  CAS  PubMed  PubMed Central  Google Scholar 

Lin MH, Li CC, Shu JC, Chu HW, Liu CC, Wu CC. Exoproteome Profiling reveals the involvement of the Foldase PrsA in the cell Surface properties and Pathogenesis of Staphylococcus aureus. Proteomics. 2018;18(5–6):e1700195. https://doi.org/10.1002/pmic.201700195.

Article  CAS  PubMed  Google Scholar 

Jousselin A, Manzano C, Biette A, Reed P, Pinho MG, Rosato AE, et al. The Staphylococcus aureus Chaperone PrsA is a new Auxiliary factor of Oxacillin Resistance affecting penicillin-binding protein 2A. Antimicrob Agents Chemother. 2016;60(3):1656–66. https://doi.org/10.1128/AAC.02333-15.

Article  CAS  PubMed Central  Google Scholar 

de Carvalho C, Taglialegna A, Rosato AE. Impact of PrsA on membrane lipid composition during daptomycin-resistance-mediated beta-lactam sensitization in clinical MRSA strains. J Antimicrob Chemother. 2021;77(1):135–47. https://doi.org/10.1093/jac/dkab356.

Article  CAS  PubMed  PubMed Central  Google Scholar 

Young BC, Wu CH, Charlesworth J, Earle S, Price JR, Gordon NC, et al. Antimicrobial resistance determinants are associated with Staphylococcus aureus bacteraemia and adaptation to the healthcare environment: a bacterial genome-wide association study. Microb Genom. 2021;7(11):000700. https://doi.org/10.1099/mgen.0.000700.

Article  CAS  PubMed  PubMed Central  Google Scholar 

Kobayashi SD, DeLeo FR. Staphylococcus aureus protein A promotes immune suppression. mBio. 2013;4(5):e00764–13. https://doi.org/10.1128/mBio.00764-13.

Article  CAS  PubMed  PubMed Central  Google Scholar 

O’Halloran DP, Wynne K, Geoghegan JA. Protein A is released into the Staphylococcus aureus culture supernatant with an unprocessed sorting signal. Infect Immun. 2015;83(4):1598–609. https://doi.org/10.1128/IAI.03122-14.

Article  CAS  PubMed  PubMed Central  Google Scholar 

Huntzinger E, Boisset S, Saveanu C, Benito Y, Geissmann T, Namane A, et al. Staphylococcus aureus RNAIII and the endoribonuclease III coordinately regulate spa gene expression. EMBO J. 2005;24(4):824–35. https://doi.org/10.1038/sj.emboj.7600572.

Article  CAS  PubMed  PubMed Central  Google Scholar 

Stephenson K, Harwood CR. Influence of a cell-wall-associated protease on production of alpha-amylase by Bacillus subtilis. Appl Environ Microbiol. 1998;64(8):2875–81.

Article  CAS  PubMed  PubMed Central  Google Scholar 

Harris LG, Foster SJ, Richards RG. An introduction to Staphylococcus aureus, and techniques for identifying and quantifying S. sureus adhesins in relation to adhesion to biomaterials: review. Eur Cell Mater. 2002;4:39–60. https://doi.org/10.22203/ecm.v004a04.

Jakob RP, Koch JR, Burmann BM, Schmidpeter PA, Hunkeler M, Hiller S, et al. Dimeric structure of the bacterial extracellular foldase PrsA. J Biol Chem. 2015;290(6):3278–92. https://doi.org/10.1074/jbc.M114.622910.

Article  CAS  PubMed  Google Scholar 

Alonzo F 3rd, Xayarath B, Whisstock JC, Freitag NE. Functional analysis of the Listeria monocytogenes secretion chaperone PrsA2 and its multiple contributions to bacterial virulence. Mol Microbiol. 2011;80(6):1530–48. https://doi.org/10.1111/j.1365-2958.2011.07665.x.

Article  CAS  PubMed  PubMed Central  Google Scholar 

Frain KM, Robinson C, van Dijl JM. Transport of folded proteins by the Tat System. Protein J. 2019;38(4):377–88. https://doi.org/10.1007/s10930-019-09859-y.

Article  CAS  PubMed  PubMed Central  Google Scholar 

Green ER, Mecsas J. Bacterial Secretion systems: an overview. Microbiol Spectr. 2016;4(1). https://doi.org/10.1128/microbiolspec.VMBF-0012-2015.

Schneewind O, Missiakas D. Sec-secretion and sortase-media

留言 (0)

沒有登入
gif