Amino acid residues 196-225 of LcrV represent a plague protective epitope

作者:Quenee Lauriane E; Berube Bryan J; Segal Joshua; Elli Derek; Ciletti Nancy A; Anderson Deborah; Schneewind Olaf*
来源:Vaccine, 2010, 28(7): 1870-1876.
DOI:10.1016/j.vaccine.2009.11.076

摘要

LcrV, a protein that resides at the tip of the type III secretion needles of Yersinia pestis, is the single most important plague protective antigen. Earlier work reported monoclonal antibody MAb 7.3, which binds a conformational epitope of LcrV and protects experimental animals against lethal plague challenge. By screening monoclonal antibodies directed against LcrV for their ability to protect immunized mice against bubonic plague challenge,we examined here the possibility of additional protective epitopes. MAb BA5 protected animals against plague, neutralized the Y. pestis type III secretion pathyway and promoted opsonophagocytic clearance of bacteria in blood. LcrV residues 196-225 were necessary and sufficient for MAb BA5 binding. Compared to full-length LcrV, a variant lacking its residues 196-225 retained the ability of eliciting plague protection. These results identify LcrV residues 196-225 as a linear epitope that is recognized by the murine immune system to confer plague protection.

  • 出版日期2010-2-17