Fimbrial Polyadhesins: Anti-immune Armament of Yersinia
The adhesive organelles play a pivotal role in the initiation of bacterial infections. The 3D structure of adhesin subunits bound to host-cell receptors and the final architecture of the fimbrial adhesive organelles of Gram-negative pathogens reveal two functional families of the organelles, respectively, possessing polyadhesive and monoadhesive binding. The F1, pH6 (Psa), and Myf antigens of Yersinia are the typical members of FGL (having a long F1–G1 loop) chaperone-assembled polyadhesins belonged to the γ3-monophyletic group. High-resolution structures of the F1 minifibers confirm that Yersinia pestis capsule is made of linearly polymerized Caf1 subunits and exploit the principle of donor-strand complementation for their polymerization. The F1 and pH6 polyadhesins contribute to the powerful anti-immune armament of Y. pestis and act in concert with the Yersinia type III secretion injectisome. The binding of F1 and pH6 polyadhesins to the specific host-cell receptors may lead to their massive aggregation that triggers suicidal proinflammatory responses.
KeywordsSurfactant Migration Arthritis Enthalpy Carbohydrate
This work was supported by grants from the European Commission/Research Executive Agency under a Marie Curie International Incoming Fellowship (235538) and a grant from the Academy of Finland (112900).
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