Antigenic structure of human respiratory syncytial virus fusion glycoprotein
JA Lopez, R Bustos, C Örvell, M Berois… - Journal of …, 1998 - Am Soc Microbiol
JA Lopez, R Bustos, C Örvell, M Berois, J Arbiza, B García-Barreno, JA Melero
Journal of virology, 1998•Am Soc MicrobiolNew series of escape mutants of human respiratory syncytial virus were prepared with
monoclonal antibodies specific for the fusion (F) protein. Sequence changes selected in the
escape mutants identified two new antigenic sites (V and VI) recognized by neutralizing
antibodies and a group-specific site (I) in the F1 chain of the F molecule. The new epitopes,
and previously identified antigenic sites, were incorporated into a refined prediction of
secondary-structure motifs to generate a detailed antigenic map of the F glycoprotein.
monoclonal antibodies specific for the fusion (F) protein. Sequence changes selected in the
escape mutants identified two new antigenic sites (V and VI) recognized by neutralizing
antibodies and a group-specific site (I) in the F1 chain of the F molecule. The new epitopes,
and previously identified antigenic sites, were incorporated into a refined prediction of
secondary-structure motifs to generate a detailed antigenic map of the F glycoprotein.
Abstract
New series of escape mutants of human respiratory syncytial virus were prepared with monoclonal antibodies specific for the fusion (F) protein. Sequence changes selected in the escape mutants identified two new antigenic sites (V and VI) recognized by neutralizing antibodies and a group-specific site (I) in the F1 chain of the F molecule. The new epitopes, and previously identified antigenic sites, were incorporated into a refined prediction of secondary-structure motifs to generate a detailed antigenic map of the F glycoprotein.
American Society for Microbiology