Flanking N- and C-terminal domains of PrsA in Streptococcus suis type 2 are crucial for inducing cell death independent of TLR2 recognition

References

• Segura M. Streptococcus suis research: progress and challenges. Pathogens. 2020;9(9):707. doi: 10.3390/pathogens9090707
   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(7):585–13. doi: 10.1016/j.tim.2017.02.005
   PubMed Web of Science ®Google Scholar
• Xia X, Qin W, Zhu H, et al. How Streptococcus suis serotype 2 attempts to avoid attack by host immune defenses. J Microbiol Immunol Infect. 2019;52(4):516–525. doi: 10.1016/j.jmii.2019.03.003
   PubMedGoogle Scholar
• Haas B, Grenier D. Understanding the virulence of Streptococcus suis: a veterinary, medical, and economic challenge. Med Mal Infect. 2018;48(3):159–166. doi: 10.1016/j.medmal.2017.10.001
   PubMed Web of Science ®Google Scholar
• Yan G, Elbadawi M, Efferth T. Multiple cell death modalities and their key features (review). World Acad Sci J. 2020. doi: 10.3892/wasj.2020.40
   Google Scholar
• Ashida H, Mimuro H, Ogawa M, et al. Cell death and infection: a double-edged sword for host and pathogen survival. J Cell Bio. 2011;195(6):931–942. doi: 10.1083/jcb.201108081
   PubMed Web of Science ®Google Scholar
• Labbé K, Saleh M. Cell death in the host response to infection. Cell Death Diff. 2008;15(9):1339–1349. doi: 10.1038/cdd.2008.91
   PubMed Web of Science ®Google Scholar
• Stephenson HN, Herzig A, Zychlinsky A. Beyond the grave: When is cell death critical for immunity to infection? Curr Opin Immunol. 2016;38:59–66. doi: 10.1016/j.coi.2015.11.004
   PubMed Web of Science ®Google Scholar
• Bertheloot D, Latz E, Franklin BS. Necroptosis, pyroptosis and apoptosis: an intricate game of cell death. Cell Mol Immunol. 2021;18(5):1106–1121. doi: 10.1038/s41423-020-00630-3
   PubMed Web of Science ®Google Scholar
• Wang Y, Kanneganti TD. From pyroptosis, apoptosis and necroptosis to PANoptosis: a mechanistic compendium of programmed cell death pathways. Computat Struct Biotechnol J. 2021;19:4641–4657. doi: 10.1016/j.csbj.2021.07.038
   PubMed Web of Science ®Google Scholar
• Tang D, Kang R, Berghe TV, et al. The molecular machinery of regulated cell death. Cell Res. 2019;29(5):347–364. doi: 10.1038/s41422-019-0164-5
   PubMed Web of Science ®Google Scholar
• Fink Susan L, Apoptosis CBT. Pyroptosis, and necrosis: mechanistic description of dead and dying eukaryotic cells. Infect Immun. 2005;73:1907–1916. doi: 10.1128/IAI.73.4.1907-1916.2005
   PubMed Web of Science ®Google Scholar
• Krysko DV, Vanden Berghe T, D’Herde K, et al. Apoptosis and necrosis: detection, discrimination and phagocytosis. Methods. 2008;44(3):205–221. doi: 10.1016/j.ymeth.2007.12.001
   PubMed Web of Science ®Google Scholar
• Wu W, Liu P, Li J. Necroptosis: an emerging form of programmed cell death. Crit Rev Oncol Hematol. 2012;82(3):249–258. doi: 10.1016/j.critrevonc.2011.08.004
   PubMed Web of Science ®Google Scholar
• Van Opdenbosch N, Lamkanfi M. Caspases in cell death, inflammation, and disease. Immunity. 2019;50(6):1352–1364. doi: 10.1016/j.immuni.2019.05.020
   PubMed Web of Science ®Google Scholar
• Bergsbaken T, Fink SL, Cookson BT. Pyroptosis: host cell death and inflammation. Nature Rev Microbiol. 2009;7(2):99–109. doi: 10.1038/nrmicro2070
   PubMed Web of Science ®Google Scholar
• Frank D, Vince JE. Pyroptosis versus necroptosis: similarities, differences, and crosstalk. Cell Death Diff. 2019;26(1):99–114. doi: 10.1038/s41418-018-0212-6
   PubMed Web of Science ®Google Scholar
• Place DE, Lee S, Kanneganti TD. Panoptosis in microbial infection. Curr Opin Microbiol. 2021;59:42–49. doi: 10.1016/j.mib.2020.07.012
   PubMed Web of Science ®Google Scholar
• Schmidpeter PAM, Schmid FX. Prolyl isomerization and its catalysis in protein folding and protein function. J Mol Biol. 2015;427(7):1609–1631. doi: 10.1016/j.jmb.2015.01.023
   PubMed Web of Science ®Google Scholar
• Schiene-Fischer C. Multidomain peptidyl prolyl cis/trans isomerases. Biochim Biophys Acta Gen Subj. 2015;1850(10):2005–2016. doi: 10.1016/j.bbagen.2014.11.012
   Web of Science ®Google Scholar
• Ünal Can M, Steinert M. Microbial peptidyl-prolyl cis/trans isomerases (PPIases): virulence factors and potential alternative drug targets. Microbiol Mol Biol Rev. 2014;78(3):544–571. doi: 10.1128/MMBR.00015-14
   PubMed Web of Science ®Google Scholar
• Sarvas M, Harwood CR, Bron S, et al. Post-translocational folding of secretory proteins in gram-positive bacteria. Biochim Biophys Acta, Mol Cell Res. 2004;1694:311–327. doi: 10.1016/j.bbamcr.2004.04.009
   PubMed Web of Science ®Google Scholar
• Vitikainen M, Lappalainen I, Seppala R, 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):19302–19314. doi: 10.1074/jbc.M400861200
   PubMed Web of Science ®Google Scholar
• Alonzo F 3rd, Port GC, Cao M, et al. The posttranslocation chaperone PrsA2 contributes to multiple facets of Listeria monocytogenes pathogenesis. Infect Immun. 2009;77(7):2612–2623. doi: 10.1128/IAI.00280-09
   PubMed Web of Science ®Google Scholar
• Leuzzi R, Serino L, Scarselli M, et al. Ng-MIP, a surface-exposed lipoprotein of Neisseria gonorrhoeae, has a peptidyl-prolyl cis/trans isomerase (PPIase) activity and is involved in persistence in macrophages. Mol Microbiol. 2005;58(3):669–681. doi: 10.1111/j.1365-2958.2005.04859.x
   PubMed Web of Science ®Google Scholar
• Guo L, Wu T, Hu W, et al. Phenotypic characterization of the foldase homologue PrsA in Streptococcus mutans. Mol Oral Microbiol. 2013;28:154–165. doi: 10.1111/omi.12014
   PubMed Web of Science ®Google Scholar
• Jiang X, Yang Y, Zhou J, et al. Roles of the putative type IV-like secretion System key component VirD4 and PrsA in pathogenesis of Streptococcus suis type 2. Front Cell Infect Microbiol. 2016;6:172. doi: 10.3389/fcimb.2016.00172
   PubMed Web of Science ®Google Scholar
• Liu H, Fu H, Jiang X, et al. PrsA contributes to Streptococcus suis serotype 2 pathogenicity by modulating secretion of selected virulence factors. Vet Microbiol. 2019;236:108375. doi: 10.1016/j.vetmic.2019.07.027
   PubMed Web of Science ®Google Scholar
• Heuck AP, Moe PC, Johnson BB. The cholesterol-dependent cytolysin family of gram-positive bacterial toxins. In: Harris J, editor. Cholesterol binding and cholesterol transport proteins: structure and function in health and disease. DordrechtNetherlands: Springer Netherlands; 2010. pp. 551–577. doi: 10.1007/978-90-481-8622-8_20
   Google Scholar
• Jiang X, Yang Y, Zhou J, et al. Peptidyl isomerase PrsA is surface-associated on Streptococcus suis and offers cross-protection against serotype 9 strain. FEMS Microbiol Lett. 2019;366(2): doi: 10.1093/femsle/fnz002
   Web of Science ®Google Scholar
• Wallberg F, Tenev T, Meier P. Analysis of apoptosis and necroptosis by fluorescence-activated cell sorting. Cold Spring Harb Protoc. 2016;2016:db prot087387. doi: 10.1101/pdb.prot087387
   Google Scholar
• Goldmann O, Sastalla I, Wos-Oxley M, et al. Streptococcus pyogenes induces oncosis in macrophages through the activation of an inflammatory programmed cell death pathway. Cell Microbiol. 2009;11(1):138–155. doi: 10.1111/j.1462-5822.2008.01245.x
   PubMed Web of Science ®Google Scholar
• Cao L, Mu W. Necrostatin-1 and necroptosis inhibition: pathophysiology and therapeutic implications. Pharmacol Res. 2021;163:105297. doi: 10.1016/j.phrs.2020.105297
   PubMed Web of Science ®Google Scholar
• de Almagro MC, Vucic D, de Almagro MC. Necroptosis: pathway diversity and characteristics. Semin Cell Dev Biol. 2015;39:56–62. doi: 10.1016/j.semcdb.2015.02.002
   PubMed Web of Science ®Google Scholar
• Lin L, Xu L, Lv W, et al. An NLRP3 inflammasome-triggered cytokine storm contributes to streptococcal toxic shock-like syndrome (STSLS). PLOS Pathogens. 2019;15(6):e1007795. doi: 10.1371/journal.ppat.1007795
   PubMed Web of Science ®Google Scholar
• Dal Peraro M, van der Goot FG. Pore-forming toxins: ancient, but never really out of fashion. Nat Rev Microbiol. 2016;14(2):77–92. doi: 10.1038/nrmicro.2015.3
   PubMed Web of Science ®Google Scholar
• Henderson B, Allan E, Coates Anthony RM. Stress wars: the direct role of host and bacterial molecular chaperones in bacterial infection. Infect Immun. 2006;74(7):3693–3706. doi: 10.1128/IAI.01882-05
   PubMed Web of Science ®Google Scholar
• Cahoon LA, Freitag NE. Listeria monocytogenes virulence factor secretion: don’t leave the cell without a chaperone. Front Cell Infect Microbiol. 2014;4:13. doi: 10.3389/fcimb.2014.00013
   PubMed Web of Science ®Google Scholar
• Ernst K, Schnell L, Barth H. Host cell chaperones Hsp70/Hsp90 and peptidyl-prolyl cis/trans isomerases are required for the membrane translocation of bacterial adp-ribosylating toxins. In: Barth H, editor. Uptake and trafficking of protein toxins. Cham: Springer International Publishing; 2017. pp. 163–198. doi: 10.1007/82_2016_14
   Google Scholar
• Basak C, Pathak SK, Bhattacharyya A, et al. The secreted peptidyl prolyl cis, trans-isomerase HP0175 of Helicobacter pylori induces apoptosis of gastric epithelial cells in a TLR4- and apoptosis signal-regulating kinase 1-dependent manner. J Immunol. 2005;174(9):5672–5680. doi: 10.4049/jimmunol.174.9.5672
   PubMed Web of Science ®Google Scholar
• Kundu M, Henderson B, editor. Moonlighting Cell Stress Proteins in Microbial Infections. Dordrecht: Springer; 2013. p. 81–91. doi: 10.1007/978-94-007-6787-4_5
   Google Scholar
• Karki R, Kanneganti TD. The ‘cytokine storm’: molecular mechanisms and therapeutic prospects. Trends Immunol. 2021;42(8):681–705. doi: 10.1016/j.it.2021.06.001
   PubMed Web of Science ®Google Scholar
• Alonzo F 3rd, Xayarath B, Whisstock JC, et al. Functional analysis of the Listeria monocytogenes secretion chaperone PrsA2 and its multiple contributions to bacterial virulence. Mol Microbiol. 2011;80(6):1530–1548. doi: 10.1111/j.1365-2958.2011.07665.x
   PubMed Web of Science ®Google Scholar
• Hyyrylainen HL, Marciniak BC, Dahncke K, et al. Penicillin-binding protein folding is dependent on the PrsA peptidyl-prolyl cis-trans isomerase in Bacillus subtilis. Mol Microbiol. 2010;77(1):108–127. doi: 10.1111/j.1365-2958.2010.07188.x
   PubMed Web of Science ®Google Scholar
• Jousselin A, Renzoni A, Andrey Diego O, et al. The posttranslocational chaperone lipoprotein prsa is involved in both glycopeptide and oxacillin resistance in staphylococcus aureus. Antimicrob Agents Chemother. 2012;56(7):3629–3640. doi: 10.1128/AAC.06264-11
   PubMed Web of Science ®Google Scholar
• Lin M-H, Li C-C, Shu J-C, et al. Exoproteome profiling reveals the involvement of the foldase prsa in the cell surface properties and pathogenesis of Staphylococcus aureus. Proteomics. 2018;18(5–6):1700195. doi: 10.1002/pmic.201700195
   PubMed Web of Science ®Google Scholar
• Wiemels Richard E, Cech Stephanie M, Meyer Nikki M, et al. An Intracellular peptidyl-prolyl cis/trans isomerase is required for folding and activity of the staphylococcus aureus secreted virulence factor nuclease. J Bacteriol. 2016;199:e00453–16. doi: 10.1128/JB.00453-16
   PubMed Web of Science ®Google Scholar
• Kawai T, Akira S. Toll-like receptors and their crosstalk with other innate receptors in infection and immunity. Immunity. 2011;34(5):637–650. doi: 10.1016/j.immuni.2011.05.006
   PubMed Web of Science ®Google Scholar
• Kawai T, Akira S. The role of pattern-recognition receptors in innate immunity: update on Toll-like receptors. Nat Immunol. 2010;11:373–384. doi: 10.1038/ni.1863
   PubMed Web of Science ®Google Scholar
• Kumar S, Ingle H, Prasad DV, et al. Recognition of bacterial infection by innate immune sensors. Crit Rev Microbiol. 2013;39:229–246. doi: 10.3109/1040841X.2012.706249
   PubMed Web of Science ®Google Scholar