Sugiyama M, Minamoto N, Kinjo T, Hirayama N, Asano K, Tsukiyama-Kohara K, Yoshikawa Y, Yamanouchi K
Department of Veterinary Public Health, Faculty of Agriculture, Gifu University, Japan.
J Gen Virol. 1991 Aug;72 ( Pt 8):1863-9. doi: 10.1099/0022-1317-72-8-1863.
A total of 24 monoclonal antibodies (MAbs) against the haemagglutinin (H) and the fusion protein (F) of rinderpest virus (RPV) were used to characterize their antigenic structure and biological properties, and to analyse natural variation in the envelope proteins of morbilliviruses. The anti-H and anti-F MAbs defined seven and three distinct antigenic sites, respectively. The MAbs to six sites on H were able to neutralize the infectivity of RPV. The addition of guinea-pig complement or anti-mouse immunoglobulin increased the virus-neutralizing antibody titre of most of the anti-H MAbs, including those lacking neutralizing activity. One of the antigenic sites on H was conserved among morbilliviruses and the MAbs to this site had haemagglutination inhibition activity against measles virus (MV). The remaining sites were specific for RPV and varied antigenically between strains of RPV. The anti-F MAbs lacked neutralizing activity, but two of the five MAbs did show activity in the presence of complement or anti-mouse immunoglobulin. On the whole, the antigenic sites on F were conserved in some strains of MV, but not in canine distemper virus. All of the sites on the surface proteins were sensitive to SDS and, although those on F were not affected by 2-mercaptoethanol, five of the seven sites on H were destroyed by it. These results suggest that the epitopes on the envelope proteins are conformation-dependent.
共使用了24种针对牛瘟病毒（RPV）血凝素（H）和融合蛋白（F）的单克隆抗体（MAb）来表征其抗原结构和生物学特性，并分析麻疹病毒包膜蛋白的自然变异。抗H和抗F单克隆抗体分别确定了7个和3个不同的抗原位点。针对H上6个位点的单克隆抗体能够中和RPV的感染性。添加豚鼠补体或抗小鼠免疫球蛋白可提高大多数抗H单克隆抗体的病毒中和抗体效价，包括那些缺乏中和活性的抗体。H上的一个抗原位点在麻疹病毒中是保守的，针对该位点的单克隆抗体对麻疹病毒（MV）具有血凝抑制活性。其余位点是RPV特有的，并且在RPV不同毒株之间存在抗原差异。抗F单克隆抗体缺乏中和活性，但五个单克隆抗体中的两个在存在补体或抗小鼠免疫球蛋白时确实表现出活性。总体而言，F上的抗原位点在某些MV毒株中是保守的，但在犬瘟热病毒中则不然。表面蛋白上的所有位点对SDS敏感，尽管F上的位点不受2-巯基乙醇影响，但H上7个位点中的5个被其破坏。这些结果表明包膜蛋白上的表位是构象依赖性的。
