Epitope mapping of the major Epstein-Barr virus outer envelope glycoprotein gp350/220.
To understand the complete immunochemical structure of the Epstein-Barr virus (EBV) major membrane glycoprotein gp350/220, monoclonal antibodies (MAbs) reacting with this important viral antigen were isolated. Through competitive inhibition binding studies, it was determined that a group of 18 IgG MAbs recognized seven distinct epitopes on the gp350/220 molecule. Eight of these MAbs fell into a single epitope group with four of those MAbs, as well as a single MAb from another epitope group, being capable of neutralizing EBV strain B95-8 transformation of umbilical cord lymphocytes.
D000911:Antibodies, Monoclonal / Q000276:immunology; D000914:Antibodies, Viral / Q000276:immunology; D000956:Antigens, Viral / Q000276:immunology*; D001667:Binding, Competitive; D002472:Cell Transformation, Viral; D000939:Epitopes / Q000276:immunology*; D004854:Herpesvirus 4, Human / Q000276:immunology*; D006801:Humans; D007231:Infant, Newborn; D008214:Lymphocytes / Q000382:microbiology; D009500:Neutralization Tests; D014470:Umbilical Cord / Q000166:cytology; D014763:Viral Matrix Proteins
D000911:Antibodies, Monoclonal; D000914:Antibodies, Viral; D000956:Antigens, Viral; C037662:EBV-associated membrane antigen, Epstein-Barr virus; D000939:Epitopes; D014763:Viral Matrix Proteins