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A conserved glycine residue of trimeric autotransporter domains plays a key role in Yersinia adhesin A autotransport.

A conserved glycine residue of trimeric autotransporter domains plays a key role in Yersinia adhesin A autotransport. Research Abstract Details 

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  • A conserved glycine residue of trimeric autotransporter domains plays a key role in Yersinia adhesin A autotransport. Abstract Text:

    ulrike grosskinskyUlrike Grosskinsky,monika Monika ,michaela fritzMichaela Fritz,yvonne schmidYvonne Schmid,marina c lamparterMarina C Lamparter,pawel szczesnyPawel Szczesny,andrei n lupasAndrei N Lupas,ingo b autenriethIngo B Autenrieth,dirk linkeDirk Linke,ulrike grosskinskyUlrike Grosskinsky,monika Monika ,michaela fritzMichaela Fritz,yvonne schmidYvonne Schmid,marina c lamparterMarina C Lamparter,pawel szczesnyPawel Szczesny,andrei n lupasAndrei N Lupas,ingo b autenriethIngo B Autenrieth,dirk linkeDirk Linke,ulrike grosskinskyUlrike Grosskinsky,monika Monika ,michaela fritzMichaela Fritz,yvonne schmidYvonne Schmid,marina c lamparterMarina C Lamparter,pawel szczesnyPawel Szczesny,andrei n lupasAndrei N Lupas,ingo b autenriethIngo B Autenrieth,dirk linkeDirk Linke,

    The Yersinia adhesin A (YadA) is a trimeric autotransporter adhesin of enteric yersiniae. It consists of three major domains: a head mediating adherence to host cells, a stalk involved in serum resistance, and an anchor that forms a membrane pore and is responsible for the autotransport function. The anchor contains a glycine residue, nearly invariant throughout trimeric autotransporter adhesins, that faces the pore lumen. To address the role of this glycine, we replaced it with polar amino acids of increasing side chain size and expressed wild-type and mutant YadA in Escherichia coli. The mutations did not impair the YadA-mediated adhesion to collagen and to host cells or the host cell cytokine production, but they decreased the expression levels and stability of YadA trimers with increasing side chain size. Likewise, autoagglutination and resistance to serum were decreased in these mutants. We found that the periplasmic protease DegP is involved in the degradation of YadA and that in an E. coli degP deletion strain, mutant versions of YadA were expressed almost to wild-type levels. We conclude that the conserved glycine residue affects both the export and the stability of YadA and consequently some of its putative functions in pathogenesis.

    A conserved glycine residue of trimeric autotransporter domains plays a key role in Yersinia adhesin A autotransport. Publishing Authors By Initials

    u grosskinskyU Grosskinsky,m M ,m fritzM Fritz,y schmidY Schmid,mc lamparterMC Lamparter,p szczesnyP Szczesny,an lupasAN Lupas,ib autenriethIB Autenrieth,d linkeD Linke,u grosskinskyU Grosskinsky,m M ,m fritzM Fritz,y schmidY Schmid,mc lamparterMC Lamparter,p szczesnyP Szczesny,an lupasAN Lupas,ib autenriethIB Autenrieth,d linkeD Linke,u grosskinskyU Grosskinsky,m M ,m fritzM Fritz,y schmidY Schmid,mc lamparterMC Lamparter,p szczesnyP Szczesny,an lupasAN Lupas,ib autenriethIB Autenrieth,d linkeD Linke,

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    A conserved glycine residue of trimeric autotransporter domains plays a key role in Yersinia adhesin A autotransport. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Journal of bacteriology

    VOLUME: 189

    Page Numbers: 9011-9

    Journal Abbreviation: J. Bacteriol.

    ISSN: 1098-5530

    DAY: 5

    MONTH: 10

    YEAR: 2007

    A conserved glycine residue of trimeric autotransporter domains plays a key role in Yersinia adhesin A autotransport. Information

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    LANGUAGE: eng

    NlmUniqueID: 2985120

    A conserved glycine residue of trimeric autotransporter domains plays a key role in Yersinia adhesin A autotransport. Keywords Mesh Terms:

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    Grant and Affiliation Information for A conserved glycine residue of trimeric autotransporter domains plays a key role in Yersinia adhesin A autotransport.

    AFFILIATION: Institut für Medizinische Mikrobiologie und Hygiene, Universitätsklinikum Tübingen, Tübingen, Germany.

    Country: United States

    United States Research PublicationUnited States Research Publication

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    MEDLINETA: J Bacteriol

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