Epitope mapping and use of epitope-specific antisera to characterize the VP5* binding site in rotavirus SA11 NSP4.

ABSTRACT: Rotavirus (RV) is the leading cause of infantile gastroenteritis worldwide. RV nonstructural protein 4 (NSP4), the first characterized viral enterotoxin, is a 28-kDa glycoprotein that has pleiotropic functions in RV infection and pathogenesis. NSP4 has multiple forms enabling it to perform its different functions. Dissecting such functions could be facilitated by use of epitope-specific antibodies. This work mapped the epitopes for the monoclonal antibody B4-2/55 and three polyclonal antisera generated against synthetic SA11 NSP4 peptides corresponding to residues 114-135, 120-147, and 150-175. The epitope for B4-2/55 mapped to residues 100-118, wherein residues E105, R108 and E111 are critical for antibody binding. Antiserum generated to two peptides (aa114-135 and aa120-147) with enterot

SUBMITTER: Hyser JM 

PROVIDER: S-EPMC2377065 | biostudies-literature | 2008 Mar

REPOSITORIES: biostudies-literature