Gonzalez-Scarano F, Shope R E, Calisher C H, Nathanson N
Prog Clin Biol Res. 1983;123:145-56.
Monoclonal antibodies against the Gl (glycoprotein) and Nc (nucleocapsid) proteins of LaCrosse (LAC) and Tahyna (TAH) viruses were generated using a standard protocol. Monoclonal antibodies against Gl were either neutralizing or non-neutralizing, and there was close concordance between inhibition of hemagglutination and neutralizing activities. The LAC virus neutralizing antibodies could be further subdivided into strain-specific and cross-reactive groups on the basis of both neutralization and inhibition of hemagglutination. These data support the concept of a glycoprotein molecule with three antigenic sites, two involved in neutralization and hemagglutination, and an additional site with no biological function as yet defined. Preliminary information from LAC virus variants selected with these monoclonal antibodies agrees with this interpretation. Anti Nc antibodies were all cross-reactive in an ELISA assay. Patterns of monoclonal cross-reactivity against California serogroup viruses are compared with the currently accepted antigenic relationships.
采用标准方案制备了抗拉克罗斯（LAC）病毒和塔希纳（TAH）病毒糖蛋白（Gl）和核衣壳（Nc）蛋白的单克隆抗体。抗Gl的单克隆抗体既有中和性的，也有非中和性的，血凝抑制活性和中和活性之间存在密切一致性。基于中和及血凝抑制试验，LAC病毒中和抗体可进一步细分为毒株特异性和交叉反应性两组。这些数据支持了这样一种概念，即糖蛋白分子有三个抗原位点，其中两个参与中和及血凝反应，另一个位点的生物学功能尚未明确。用这些单克隆抗体筛选出的LAC病毒变异株的初步信息与这一解释相符。在ELISA试验中，抗Nc抗体均具有交叉反应性。将针对加利福尼亚血清群病毒的单克隆交叉反应模式与目前公认的抗原关系进行了比较。
