Epitopes of the G1 glycoprotein of La Crosse virus form overlapping clusters within a single antigenic site.
Epitopes of the G1 glycoprotein of La Crosse virus form overlapping clusters within a single antigenic site.
复制标题
拉克罗斯病毒 G1 糖蛋白的表位在单个抗原位点内形成重叠的簇。
DOI:
10.1016/0042-6822(85)90283-1
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发表时间:
1985
期刊:
影响因子:
3.7
通讯作者:
Gonzalez-Scarano,F
中科院分区:
文献类型:
--
作者:
Najjar,JA;Gentsch,JR;Nathanson,N;Gonzalez-Scarano,F
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),Virology120, 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 nonneutralizing antigenic site on the G1 protein.