Epitopes of the G1 glycoprotein of La Crosse virus form overlapping clusters within a single antigenic site.
Antigenic sites on the G1 glycoprotein of La Crosse bunyavirus were defined by constructing a panel of neutralizing and nonneutralizing monoclonal antibodies (F. Gonzalez-Scarano, R. E. Shope, C. H. Calisher, and N. Nathanson (1982), Virology 120, 42-53). To analyze the relationship between the individual epitopes delineated by monoclonal antibodies, 11 neutralizing antibodies were used to select variant viruses. These variant viruses were tested against the panel of anti-G1 protein monoclonal antibodies by neutralization and by ELISA. The neutralization tests assigned the 11 epitopes to five groups, consisting of 6, 2, 1, 1, and 1 epitopes. ELISA tests gave a similar pattern, but also demonstrated interrelationships between four of the five epitope groups, suggesting that there may be a single immunodominant antigenic site on the G1 protein. When eight nonneutralizing anti-G1 monoclonal antibodies were tested in ELISA, they fell into three of the five epitope groups defined by neutralization; there was no evidence of a separate noneutralizing antigenic site on the G1 protein.
Najjar
J A
JA
Gentsch
J R
JR
Nathanson
N
N
Gonzalez-Scarano
F
F
D000911:Antibodies, Monoclonal; D000956:Antigens, Viral / Q000032:analysis*; D002043:Bunyaviridae / Q000276:immunology*; D002141:Encephalitis Virus, California / Q000276:immunology*; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes; D006023:Glycoproteins / Q000276:immunology; D009500:Neutralization Tests
D000911:Antibodies, Monoclonal; D000956:Antigens, Viral; D000939:Epitopes; D006023:Glycoproteins