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A Conserved Glycine Residue of Trimeric Autotransporter Domains Plays a Key Role in Yersinia Adhesin A Autotransport

Ulrike Grosskinsky,^1, Monika Schütz,^1, Michaela Fritz,¹ Yvonne Schmid,¹ Marina C. Lamparter,² Pawel Szczesny,^2,3 Andrei N. Lupas,^2* Ingo B. Autenrieth,¹ and Dirk Linke²

Institut für Medizinische Mikrobiologie und Hygiene, Universitätsklinikum Tübingen, Tübingen, Germany,¹ Max Planck Institute for Developmental Biology, Department Protein Evolution, Tübingen, Germany,² Department of Bioinformatics, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland³

Received 21 June 2007/ Accepted 25 September 2007

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.

Published ahead of print on 5 October 2007.

These authors contributed equally to this study.

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