Antigenic variance.
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Antibodies, Monoclonal↗
Biomedical subjects
L Kingsford
Publications and source records attributed to L Kingsford.
Effects of specific monoclonal antibodies on La Crosse virus neutralization: aggregation, inactivation by Fab fragments, and inhibition of attachment to baby hamster kidney cells.
At high concentrations, several monoclonal antibodies to the G1 glycoprotein of La Crosse (LAC) virus aggregated the virus. To determine whether this accounted for the neutralization, the monoclonal antibodies were digested to make Fab fragments. With one exception, each monovalent antibody neutralized LAC virus to the same extent that bivalent antibody did, although higher concentrations were needed. Fab fragments of synergistic pairs of antibodies also exhibited enhanced binding in a competition binding assay but did not increase neutralization. To determine specific mechanisms for neutralization, the effects of polyclonal or monoclonal antibodies on virus attachment were examined. Polyclonal antibody to LAC virus reduced virus attachment by only 68% although it neutralized 99.99% of the virus. When virus was preincubated with a neutralizing monoclonal antibody to each of seven antigenic regions on G1, only antibody to one region reduced attachment of virus by as much as 92%. Antibodies to two regions that neutralize virus by 90-98% only inhibited attachment by 9 and 13%, respectively. The other antibodies showed intermediate degrees of neutralization and inhibition of attachment. Pairs of antibodies previously shown to be synergistic in neutralizing activity did not inhibit attachment any more than the single antibodies did.
Animals↗
Monoclonal antibodies specific for the G1 glycoprotein of La Crosse virus that react with other California serogroup viruses.
Various degrees of cross-reactivity have been observed among members of the California serogroup of bunyaviruses. Since the G1 glycoprotein of La Crosse (LAC) virus, a member of this serogroup, has been shown to contain the antigenic determinants involved in neutralization, monoclonal antibodies to this glycoprotein were used in enzyme immunosorbent and kinetics of neutralization assays with the other California viruses to detect cross-reactive sites that may be involved in neutralization. The results first indicated that five of the antigenic regions previously mapped on the LAC G1 glycoprotein contained overlapping epitopes within them. In all, a total of 16 epitopes within eight antigenic regions were identified on the G1 glycoprotein of LAC virus. One epitope was found on all of the California viruses and is therefore a group-specific antigenic determinant. A LAC-specific epitope was also identified. Different patterns of reactivity were observed among the California viruses for the rest of the antibodies. When the monoclonal antibodies (MAbs) were assayed with the uncloned reference strain of LAC and with two New York isolates, differences were found for epitopes within two antigenic regions. With one exception (snowshoe hare virus, a variety of LAC), pairs of antibodies shown to enhance neutralization of LAC virus did not increase neutralization of the other California viruses having the corresponding pairs of epitopes.
Animals↗