Nestorowicz A, Tregear G W, Southwell C N, Martyn J, Murray J M, White D O, Jackson D C
Mol Immunol. 1985 Feb;22(2):145-54. doi: 10.1016/s0161-5890(85)80008-0.
A number of peptides of the hemagglutinin (HA) of X-31 influenza virus have been synthesised. The amino acid sequences of some of these peptides represent regions of HA which have been postulated [Wiley et al., Nature, Lond. 289, 373-378 (1981)] to form the antigenic sites of this molecule. Animals were immunized with free peptide or peptide conjugated to a carrier and the resulting antisera examined for their capacities to bind to homologous peptide, whole HA, reduced and alkylated HA, and intact virus. Not all peptides examined in this way were immunogenic. Only antibodies raised against the C-terminus of HA1 peptide displayed binding to virus. This antiserum bound to the intact HA but not to the reduced and alkylated form of the molecule. These results raise questions as to the feasibility of using synthetic peptides of the influenza HA in short linear sequences to elicit neutralising antibody.
已经合成了X-31流感病毒血凝素（HA）的多种肽段。其中一些肽段的氨基酸序列代表了HA的特定区域，据推测[威利等人，《自然》，伦敦，289卷，373 - 378页（1981年）]这些区域构成了该分子的抗原位点。用游离肽或与载体偶联的肽对动物进行免疫，并检测所得抗血清与同源肽、完整HA、还原烷基化的HA以及完整病毒的结合能力。并非所有以这种方式检测的肽都具有免疫原性。只有针对HA1肽C末端产生的抗体表现出与病毒的结合。这种抗血清与完整的HA结合，但不与该分子的还原烷基化形式结合。这些结果引发了关于使用流感HA短线性序列的合成肽来引发中和抗体的可行性的问题。
