Suzuki Y
University of Shizuoka, School of Pharmaceutical Sciences, Japan.
Yakugaku Zasshi. 1993 Aug;113(8):556-78. doi: 10.1248/yakushi1947.113.8_556.
Influenza A, B viruses contain 2 viral specific, membrane associated glycoprotein antigens, hemagglutinin and sialidase. Hemagglutinin is essential for the initial binding of the virus to the cell membrane receptors that contain sialic acid such as gangliosides and sialo-glycoproteins. Hemagglutinin is also important for the intracellular viral uncoating by the low pH fusion processes. The evolution of the influenza viruses and host range variation come from the mutation of hemagglutinin and sialidase genes and change of their sialo-sugar chain recognition together with alteration in the antigenic epitopes. In this report, the molecular mechanism of the relationship between the evolutional change of the viral glycoproteins, especially hemagglutinin molecules and the change of the receptor binding specificity is reported, and also the strategy for the development of a new universal vaccine which generates the antibody whose supervariable region mimics the common receptor sialo-sugar chains for all the subtypes of influenza viruses is also described.
甲型和乙型流感病毒含有两种病毒特异性的、与膜相关的糖蛋白抗原，即血凝素和唾液酸酶。血凝素对于病毒最初与含有唾液酸的细胞膜受体（如神经节苷脂和唾液酸糖蛋白）结合至关重要。血凝素对于通过低pH融合过程进行细胞内病毒脱壳也很重要。流感病毒的进化和宿主范围变异源于血凝素和唾液酸酶基因的突变、它们对唾液酸糖链识别的改变以及抗原表位的变化。在本报告中，报道了病毒糖蛋白，尤其是血凝素分子的进化变化与受体结合特异性变化之间关系的分子机制，还描述了开发新型通用疫苗的策略，该疫苗可产生其超变区模拟所有流感病毒亚型共同受体唾液酸糖链的抗体。
