ANTIGENIC STRUCTURE OF THE HEMAGGLUTININ OF INFLUENZA VIRUS-B HONG-KONG 8/73 AS DETERMINED FROM GENE SEQUENCE-ANALYSIS OF VARIANTS SELECTED WITH MONOCLONAL-ANTIBODIES
ANTIGENIC STRUCTURE OF THE HEMAGGLUTININ OF INFLUENZA VIRUS-B HONG-KONG 8/73 AS DETERMINED FROM GENE SEQUENCE-ANALYSIS OF VARIANTS SELECTED WITH MONOCLONAL-ANTIBODIES
复制标题
DOI：
10.1016/0042-6822(84)90384-2
复制
发表时间：
1984-01-01
期刊：
影响因子：
3.7
通讯作者：
AIR, GM
中科院分区：
文献类型：
--
作者：
HOVANEC, DL;AIR, GM
乙型流感病毒的抗原变异在几个方面与甲型流感病毒不同。尚未观察到抗原转移，乙型流感的不同抗原变体共同循环，并且抗原相似的病毒相隔多年分离。为了研究B型流感病毒的抗原漂移机制，使用单克隆抗体选择B/香港/8/73病毒血凝素(HA)的抗原变异体。对 B/香港/8/73 的 HA 基因和 8 个变体的核苷酸序列进行分析，确定了 B 型流感 HA 分子中涉及抗原性的特定区域，并使抗原图谱数据与蛋白质结构相关联。与 A/Aichi/2/68 的 HA 相比，变体中改变的氨基酸出现在先前为 A 型病毒确定的 4 个抗原区域中的 2 个区域中。 8 个变体中的 4 个显示出多个核苷酸变化，其中一些导致双氨基酸变化。在本研究中，属于相同抗原基团的单克隆抗体识别对应于H3 HA的抗原位点A和B的区域中的氨基酸变化。这些结果与 A/Memphis/1/71 病毒的 HA 变体获得的结果形成对比。在甲型流感研究中，仅发现单个氨基酸的变化，并且这些变化与 3 维结构密切相关；识别1个区域的单克隆抗体不识别任何其他抗原位点。显然，虽然乙型流感HA的基本3维结构可能与甲型病毒相似，但乙型流感HA分子可能以更紧凑的方式折叠，使得抗原位点A和B比H3结构中的彼此更接近。
Antigenic variation among influenza B viruses is different from that of influenza A in several ways. Antigenic shift has not been observed, distinct antigenic variants of influenza B cocirculate, and antigenically similar viruses were isolated many years apart. To study the mechanism of antigenic drift in influenza B viruses, monoclonal antibodies were used to select antigenic variants of B/Hong Kong/8/73 virus hemagglutinin (HA). Analyses of the nucleotide sequences of the HA gene of B/Hong Kong/8/73 and the 8 variants identified specific regions of the influenza B HA molecule involved in antigenicity, and enabled antigenic mapping data to be correlated with the structure of the protein. The altered amino acids in the variants, when compared to the HA of A/Aichi/2/68, were found in 2 of the 4 antigenic regions previously identified for type A viruses. Four of the 8 variants showed multiple nucleotide changes some of which gave rise to double amino acid changes. In the present study monoclonal antibodies which belong to the same antigenic group recognize amino acid changes in regions corresponding to antigenic sites A and B of the H3 HA. These results are in contrast to those obtained with HA variants of A/Memphis/1/71 virus. In the influenza A studies only single amino acid changes were found and these correlated well with the 3-dimensional structure; monoclonal antibodies which recognized 1 region did not recognize any of the other antigenic sites. Evidently, although the basic 3-dimensional structure of the influenza B HA may be similar to that of A viruses, the B HA molecule may be folded in a more compact manner so that antigenic sites A and B are in closer proximity to each other than in the H3 structure.