Protein Domain : Outer membrane adhesion, Yersinia IPR008126

Type	Family
Description	The genus Yersinia contains just three species: Yersinia enterocolitica, Yersinia pestis, and Yersinia pseudotuberculosis [ ]. Although the three use different routes to infect their host, each targets the lymphoid tissue for invasion, and all have developed specific systems to evade host immune cells []. PYV, a major virulence plasmid common to all members of this family, harbours the genes necessary for type III secretion in the host and the exotoxins translocated by them. One of the proteins encoded within this plasmid is the Yersinia YadA non-fimbrial adhesin, a moiety that facilitates cell interaction between the host and pathogen [ ]. Mutational studies indicate that this protein allows intimate attachment and subsequent uptake by host macrophages of the bacterial cell. Synergistic mechanisms by two other PYV-encoded proteins,YopH and YopE, inhibit the action of YadA. Electron microscopy of the mature YadA adhesins suggest that they form distinct "lollipop"shaped structures on the cell surface []. This is a trait shared by the adhesins of another pathogen, namely Moraxella catarrhalis UspA1 and UspA2 []. The YadA protein itself exists as a homotrimer of 45kDa subunits, anchored in the outer bacterial membrane by its C terminus []. The lollipop's globular head is formed by the N terminus in the extracellular space. A Yersinia bacterial cell thus coated with YadA can bind a number of host cell macromolecules, including collagen, laminin, mucus and fibronectin, enhancing its capacity for infection.
Short Name	OM_adhesion_Yersinia