Structure and sequence analysis of Yersinia YadA and Moraxella UspAs reveal a novel class of adhesins

The non-fimbrial adhesins, YadA of enteropathogenic Yersinia species, and U spA1 and UspA2 of Moraxella catarrhalis, are established pathogenicity fact ors. In electron micrographs, both surface proteins appear as distinct 'lol lipop'-shaped structures forming a novel type of surface projection on the outer membranes. These structures, amino acid sequence analysis of these mo lecules and yadA gene manipulation suggest a tripartite organization: an N- terminal oval head domain is followed by a putative coiled-coil rod and ter minated by a C-terminal membrane anchor domain. In YadA, the head domain is involved in autoagglutination and binding to host cells and collagen. Anal ysis of the coiled-coil segment of YadA revealed unusual pentadecad repeats with a periodicity of 3.75, which differs significantly from the 3.5 perio dicity found in the Moraxella UspAs and other canonical coiled coils. These findings predict that the surface projections are formed by oligomers cont aining right- (Yersinia) or left-handed (Moraxella) coiled coils, Strikingl y, sequence comparison revealed that related proteins are found in many pro teobacteria, both human pathogenic and environmental species, suggesting a common role in adaptation to specific ecological niches.