Interaction Between Yersinia pestis Ail Outer Membrane Protein and the C-Terminal Domain of Human Vitronectin

Yersinia pestis, the causative agent of plague, is capable to evade human immune system response by recruiting the plasma circulating vitronectin proteins, which acts as a shield and avoids its lysis. Vitronectin recruitment is mediated by its interaction with the bacterial transmembrane protein Ail, protruding from Y. pestis outer membrane. By using all atom long-scale molecular dynamic simulations of Ail embedded in a realistic model of the bacterial membrane, we have shown that vitronectin forms a stable complex, mediated by interactions between the disordered moieties of the two proteins. The main amino acids driving the complexation have also been evidenced, thus favoring the possible rational design of specific peptides which, by inhibiting vitronectin recruitment, could act as original antibacterial agents. TOC ABSTRACT O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=186 SRC="FIGDIR/small/574511v1_ufig1.gif" ALT="Figure 1"> View larger version (140K): org.highwire.dtl.DTLVardef@1f43519org.highwire.dtl.DTLVardef@1ca1b0forg.highwire.dtl.DTLVardef@1b68510org.highwire.dtl.DTLVardef@1d9fe1d_HPS_FORMAT_FIGEXP M_FIG C_FIG