Antigenic structure of the haemagglutinin of human influenza A/H2N2 virus
Antigenic structure of the haemagglutinin of human influenza A/H2N2 virus
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DOI：
10.1099/0022-1317-82-10-2475
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发表时间：
2001-10-01
影响因子：
3.8
通讯作者：
Nakamura, K
中科院分区：
文献类型：
--
作者：
Tsuchiya, E;Sugawara, K;Nakamura, K
用19种抗A/Kayano/57血凝素（HA）的单克隆抗体（MAbs）分析了A/H2 N2流感病毒HA的抗原结构。将抗体分为三组：组I具有血凝抑制和中和活性，组II具有中和活性但没有血凝抑制活性，组III没有活性。逃逸突变体的分析选择的每一个组I和II抗体确定了六个不同的抗原位点：四个（I-A至I-D）被识别的组I单克隆抗体和两个（II-A和II-B）被识别的组II单克隆抗体。逃逸突变体的HA基因的序列分析表明，位点I-A、I-B和I-C形成了一个连续的抗原区，该抗原区含有与H3分子上的抗原位点A、B和D相对应的区域，并且位点I-D和II-B分别是位点E和C的等价物，这表明H2分子的抗原结构与H3分子的抗原结构很大程度上相似。然而，H2分子与H3分子的不同之处在于在茎域中具有高度保守的抗原位点（II-A）。还发现，由针对位点I-A、I-B和I-C的抗体选择的大多数逃逸突变体分别在位置160、187或131处获得了新的糖基化位点，这表明A/H2 N2病毒具有在HA尖端获得至少一个额外的寡糖的潜力，尽管这在其在人类中循环的11年期间从未发生过。
The antigenic structure of influenza A/H2N2 virus haemagglutinin (HA) was analysed using 19 monoclonal antibodies (MAbs) against the HA of A/Kayano/57. The antibodies were classified into three groups: group I had both haemagglutination inhibition and neutralization activities, group II had neutralization activity but no haemagglutination inhibition activity and group III had neither activity. Analysis of escape mutants selected by each of the group I and II antibodies identified six distinct antigenic sites: four (I-A to I-D) were recognized by group I MAbs and two (II-A and II-B) were recognized by group II MAbs. Sequence analysis of the HA genes of the escape mutants demonstrated that sites I-A, I-B and I-C form a contiguous antigenic area that contains the regions corresponding to antigenic sites A, B and D on the H3 molecule and that sites I-D and II-B are the equivalents of sites E and C, respectively, suggesting that the antigenic structure of the H2 molecule is largely similar to that of the H3 molecule. However, the H2 molecule differed from the H3 molecule in having a highly conserved antigenic site (II-A) in the stem domain. It was also found that most of the escape mutants selected by antibodies to sites I-A, I-B and I-C acquired a new glycosylation site at position 160, 187 or 131, respectively, which indicates that A/H2N2 viruses have the potential to gain at least one additional oligosaccharide on the tip of the HA, although this has never occurred during 11 years of its circulation in humans.