Epitopes functional in neutralization of varicella-zoster virus.
By competition neutralization assay using monoclonal antibodies (MAbs) to varicella-zoster virus (VZV) glycoproteins (gps), we attempted to determine the topographical relationship of epitopes which are functional in VZV neutralization. MAbs against gpI interfered moderately to strongly with neutralization of MAbs against gpIII, and one antigenic domain with two distinct epitopes was identified on gpIII. Competition neutralization assays performed with MAbs to gpI revealed at least three distinct antigenic domains: the first contained two complement-dependent neutralizing epitopes; the second contained five complement-dependent neutralizing, overlapping epitopes and one nonneutralizing, nonoverlapping epitope; and the third contained one complement-enhanced neutralizing epitope. Competition neutralization assays performed with MAbs to gpIV showed one antigenic domain with two distinct epitopes which competed with nonneutralizing gpI MAbs. gpII did not interfere with neutralization of gpI, gpIII, or gpIV. Our data suggest that neutralizing and nonneutralizing MAbs can interfere with the action of viral neutralization either by inhibition or by enhancement. This report describes the epitope mapping of VZV gps by a functional biological assay.
Viral and Rickettsial Disease Laboratory, California State Department of Health Services, Berkeley 94704.
B
B
Forghani
K W
KW
Dupuis
N J
NJ
Schmidt
D000911:Antibodies, Monoclonal; D000956:Antigens, Viral; D001667:Binding, Competitive; D000939:Epitopes; D006023:Glycoproteins / Q000276:immunology; D014645:Herpesvirus 3, Human / Q000276:immunology*; D009500:Neutralization Tests; D014764:Viral Proteins / Q000276:immunology
D000911:Antibodies, Monoclonal; D000956:Antigens, Viral; D000939:Epitopes; D006023:Glycoproteins; D014764:Viral Proteins