对人副流感3型病毒融合蛋白具有合胞体抑制和中和作用的单克隆抗体所识别的氨基酸的鉴定
Identification of amino acids recognized by syncytium-inhibiting and neutralizing monoclonal antibodies to the human parainfluenza type 3 virus fusion protein.
作者信息
Coelingh K V, Tierney E L
机构信息
Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20892.
出版信息
J Virol. 1989 Sep;63(9):3755-60. doi: 10.1128/JVI.63.9.3755-3760.1989.
Abstract
Neutralizing monoclonal antibodies specific for the fusion (F) glycoprotein of human parainfluenza type 3 virus (PIV3) were used to select neutralization-resistant antigenic variants. Sequence analysis of the F genes of the variants indicated that their resistance to antibody binding, antibody-mediated neutralization or to both was a result of specific amino acid substitutions within the neutralization epitopes of the F1 and F2 subunits. Comparison of the locations of PIV3 neutralization epitopes with those of Newcastle disease and Sendai viruses indicated that the antigenic organization of the fusion proteins of paramyxoviruses is similar. Furthermore, some of the PIV3 epitopes recognized by syncytium-inhibiting monoclonal antibodies are located in an F1 cysteine cluster region which corresponds to an area of the measles virus F protein involved in fusion activity.
摘要
使用针对人副流感3型病毒（PIV3）融合（F）糖蛋白的中和单克隆抗体来筛选抗中和抗原变体。对这些变体的F基因进行序列分析表明，它们对抗体结合、抗体介导的中和或两者的抗性是F1和F2亚基中和表位内特定氨基酸取代的结果。将PIV3中和表位的位置与新城疫病毒和仙台病毒的位置进行比较表明，副粘病毒融合蛋白的抗原结构相似。此外，一些被抑制合胞体的单克隆抗体识别的PIV3表位位于F1半胱氨酸簇区域，该区域对应于麻疹病毒F蛋白参与融合活性的区域。
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