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dc.contributor.authorLiu, Mengyao
dc.contributor.authorZhu, Hui
dc.contributor.authorLi, Jinquan
dc.contributor.authorGarcia, C. C.
dc.contributor.authorFeng, Wenchao
dc.contributor.authorKirpotina, Liliya N.
dc.contributor.authorHilmer, Jonathan K.
dc.contributor.authorTavares, L. P.
dc.contributor.authorLayton, A. W.
dc.contributor.authorQuinn, Mark T.
dc.contributor.authorBothner, Brian
dc.contributor.authorTeixeira, M. M.
dc.contributor.authorLei, Benfang
dc.identifier.citationLiu M., Zhu H, Li J, Garcia CC, Feng W, Kirpotina LN, Hilmer J, Tavares LP, Layton AW, Quinn MT, Bothner B, Teixeira MM, Lei B. 2012. Group A Streptococcus Secreted Esterase Hydrolyzes Platelet-Activating Factor to Impede Neutrophil Recruitment and Facilitate Innate Immune Evasion. PLoS Pathog 8(4): e1002624. PMCID: PMC3320582.en_US
dc.description.abstractThe innate immune system is the first line of host defense against invading organisms. Thus, pathogens have developed virulence mechanisms to evade the innate immune system. Here, we report a novel means for inhibition of neutrophil recruitment by Group A Streptococcus (GAS). Deletion of the secreted esterase gene (designated sse) in M1T1 GAS strains with (MGAS5005) and without (MGAS2221) a null covS mutation enhances neutrophil ingress to infection sites in the skin of mice. In trans expression of SsE in MGAS2221 reduces neutrophil recruitment and enhances skin invasion. The sse deletion mutant of MGAS5005 (ΔsseMGAS5005) is more efficiently cleared from skin than the parent strain. SsE hydrolyzes the sn-2 ester bond of platelet-activating factor (PAF), converting biologically active PAF into inactive lyso-PAF. KM and kcat of SsE for hydrolysis of 2-thio-PAF were similar to those of the human plasma PAF acetylhydrolase. Treatment of PAF with SsE abolishes the capacity of PAF to induce activation and chemotaxis of human neutrophils. More importantly, PAF receptor-deficient mice significantly reduce neutrophil infiltration to the site of ΔsseMGAS5005 infection. These findings identify the first secreted PAF acetylhydrolase of bacterial pathogens and support a novel GAS evasion mechanism that reduces phagocyte recruitment to sites of infection by inactivating PAF, providing a new paradigm for bacterial evasion of neutrophil responses.en_US
dc.subjectHealth sciencesen_US
dc.subjectCellular biologyen_US
dc.titleGroup A Streptococcus Secreted Esterase Hydrolyzes Platelet-Activating Factor to Impede Neutrophil Recruitment and Facilitate InnateImmune Evasionen_US
mus.citation.journaltitlePLoS Pathogensen_US
mus.identifier.categoryHealth & Medical Sciencesen_US
mus.identifier.categoryLife Sciences & Earth Sciencesen_US
mus.relation.collegeCollege of Letters & Scienceen_US
mus.relation.departmentChemistry & Biochemistry.en_US
mus.relation.universityMontana State University - Bozemanen_US
mus.contributor.orcidBothner, Brian|0000-0003-1295-9609en_US
mus.contributor.orcidQuinn, Mark T.|0000-0001-8114-5073en_US

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