Jackson D C, Tang X L, Brown L E, Murray J M, White D O, Tregear G W
Virology. 1986 Dec;155(2):625-32. doi: 10.1016/0042-6822(86)90222-9.
A synthetic peptide comprising the C-terminal 24 amino acids of the heavy chain (HA1) of influenza virus hemagglutinin was constructed and examined for antigenic and immunogenic activity. Monoclonal antibodies as well as polyclonal antisera raised against the synthetic peptide were able to bind to intact virus. This binding was greatly enhanced if the virus was first subjected to pH 5, suggesting that this treatment exposes the C-terminus of HA1. Using synthetic analogs of the native sequence it was shown that the epitope recognized by one of the monoclonal antibodies encompasses one or more of the C-terminal four amino acids of HA1 (residues 325-328), which are conserved within subtypes but differ between subtypes, while the other monoclonal antibody recognizes a different epitope which involves at least one of the five variable residues at positions 311-315.
构建了一种包含流感病毒血凝素重链（HA1）C末端24个氨基酸的合成肽，并对其抗原性和免疫原性活性进行了检测。针对该合成肽产生的单克隆抗体以及多克隆抗血清能够与完整病毒结合。如果病毒首先在pH 5条件下处理，这种结合会大大增强，这表明这种处理暴露了HA1的C末端。使用天然序列的合成类似物表明，一种单克隆抗体识别的表位包含HA1的C末端四个氨基酸中的一个或多个（残基325 - 328），这些氨基酸在各亚型内保守，但在不同亚型之间存在差异，而另一种单克隆抗体识别不同的表位，该表位涉及位置311 - 315处五个可变残基中的至少一个。
