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          Institute: MPI für Entwicklungsbiologie     Collection: Abteilung 1 - Protein Evolution (A. Lupas)     Display Documents

ID: 561551.0, MPI für Entwicklungsbiologie / Abteilung 1 - Protein Evolution (A. Lupas)
Trimer Stability of YadA Is Critical for Virulence of Yersinia enterocolitica
Authors:Schutz, M.; Weiss, E. M.; Schindler, M.; Hallstrom, T.; Zipfel, P. F.; Linke, D.; Autenrieth, I. B.
Date of Publication (YYYY-MM-DD):2010-06
Title of Journal:Infection and Immunity
Issue / Number:6
Start Page:2677
End Page:2690
Review Status:not specified
Audience:Not Specified
Abstract / Description:Yersinia adhesin A (YadA) is a trimeric autotransporter adhesin with multiple functions in host-pathogen interactions. The aim of this study was to dissect the virulence functions promoted by YadA in vitro and in vivo. To accomplish this, we generated Yersinia enterocolitica O: 8 mutants expressing point mutations in YadA G389, a highly conserved residue in the membrane anchor of YadA, and analyzed their impact on YadA expression and virulence functions. We found that point mutations of YadA G389 led to impaired transport, stability, and surface display of YadA. YadA G389A and G389S mutants showed comparable YadA surface expression, autoagglutination, and adhesion to those of wild-type YadA but displayed reduced trimer stability and complement resistance in vitro and were 10- to 1,000-fold attenuated in experimental Y. enterocolitica infection in mice. The G389T, G389N, and G389H mutants lost trimer stability, exhibited strongly reduced surface display, autoagglutination, adhesion properties, and complement resistance, and were avirulent (> 10,000-fold attenuation) in mice. Our data demonstrate that G389 is a critical residue of YadA, required for optimal trimer stability, transport, surface display, and serum resistance. We also show that stable trimeric YadA protein is essential for virulence of Y. enterocolitica.
Free Keywords:nf-kappa-b; human-factor h; adhesin yada; serum resistance; collagen-binding; signaling responses; complement evasion; epithelial-cells; protein; autotransporter
External Publication Status:published
Document Type:Article
Affiliations:MPI für Entwicklungsbiologie/Abteilung 1 - Proteinevolution (Andrei Lupas)
External Affiliations:Univ Tubingen Hosp, Inst Med Microbiol & Hyg, Elfriede Aulhornstr 6, D-72076 Tubingen, Germany Univ Tubingen Hosp, Inst Med Microbiol & Hyg, D-72076 Tubingen, Germany Hans Knoell Inst, Leibniz Inst Nat Prod Res & Infect Biol, D-07745 Jena, Germany Max Planck Inst Dev Biol, Dept Prot Evolut, D-72076 Tubingen, Germany %G English
Identifiers:ISSN:0019-9567 [ID No:1]
ISI:000277841300031 [ID No:2]
ISI:000277841300031 [ID No:3]
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