title: Structure and sequence analysis of Yersinia YadA and Moraxella UspAs reveal a novel class of adhesins.
abstract: The non-fimbrial adhesins, YadA of enteropathogenic Yersinia species, and UspA1 and UspA2 of Moraxella catarrhalis, are established pathogenicity factors. In electron micrographs, both surface proteins appear as distinct 'lollipop'-shaped structures forming a novel type of surface projection on the outer membranes. These structures, amino acid sequence analysis of these molecules and yadA gene manipulation suggest a tripartite organization: an N-terminal oval head domain is followed by a putative coiled-coil rod and terminated by a C-terminal membrane anchor domain. In YadA, the head domain is involved in autoagglutination and binding to host cells and collagen. Analysis of the coiled-coil segment of YadA revealed unusual pentadecad repeats with a periodicity of 3.75, which differs significantly from the 3.5 periodicity found in the Moraxella UspAs and other canonical coiled coils. These findings predict that the surface projections are formed by oligomers containing right- (Yersinia) or left-handed (Moraxella) coiled coils. Strikingly, sequence comparison revealed that related proteins are found in many proteobacteria, both human pathogenic and environmental species, suggesting a common role in adaptation to specific ecological niches.
authors.affiliation: Max von Pettenkofer-Institute for Hygiene and Medical Microbiology, Ludwig Maximilians University Munich, Pettenkoferstrabetae 9a, D-80336 München, Germany.
authors.forename: E
authors.initials: E
authors.lastname: Hoiczyk
authors.forename: A
authors.initials: A
authors.lastname: Roggenkamp
authors.forename: M
authors.initials: M
authors.lastname: Reichenbecher
authors.forename: A
authors.initials: A
authors.lastname: Lupas
authors.forename: J
authors.initials: J
authors.lastname: Heesemann
mesh_terms: D018829:Adhesins, Bacterial / Q000737:chemistry* / Q000235:genetics* / Q000648:ultrastructure; D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000235:genetics* / Q000648:ultrastructure; D002462:Cell Membrane / Q000737:chemistry / Q000648:ultrastructure; D005798:Genes, Bacterial; D006801:Humans; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D001936:Moraxella catarrhalis / Q000737:chemistry* / Q000235:genetics* / Q000648:ultrastructure; D009154:Mutation; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D014774:Virulence; D015008:Yersinia enterocolitica / Q000737:chemistry* / Q000235:genetics* / Q000648:ultrastructure
chemical_list: D018829:Adhesins, Bacterial; D001425:Bacterial Outer Membrane Proteins; C089675:UspA protein, Moraxella catarrhalis; C064832:YadA protein, Yersinia