作者: Weicen Liu , Jun Ren , Jinlong Zhang , Xiaohong Song , Shuling Liu
DOI: 10.1371/JOURNAL.PONE.0177012
关键词: Linear epitope 、 Antibody 、 Biology 、 Conformational epitope 、 Binding site 、 Yersinia pestis 、 Virology 、 Monoclonal antibody 、 Western blot 、 Epitope 、 General Biochemistry, Genetics and Molecular Biology 、 General Agricultural and Biological Sciences 、 General Medicine
摘要: Yersinia pestis (Y. pestis) has caused an alarming number of deaths throughout recorded human history, and novel prophylactics therapeutics are necessary given its potential as a bioweapon. Only one monoclonal antibody been identified to date that provides complete protection against Y. pestis. Here, we describe second murine (F2H5) provided 141 infection when administered prophylactically Balb/c mice (100 μg intravenously). We humanized F2H5, characterized ability bind the F1 protein further neutralizing epitope using computational experimental approaches. While Western blot results suggested linear epitope, peptide mapping ELISA failed identify suggesting conformational instead. adopted approach based on Residue Contact Frequency predict site antigen-antibody interaction defined F2H5/F1 binding computationally. Based approach, determined residues G104E105N106 in were critical F2H5 CDRH2 CDRH3 interacted with F1. Our show combining can effectively epitopes.