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通过针对糖多肽HA1和HA2的单克隆抗体检测到的流感病毒血凝素在酸性pH值下的变化。

Changes in the influenza virus haemagglutinin at acid pH detected by monoclonal antibodies to glycopolypeptides HA1 and HA2.

作者信息

Kostolansky F, Russ G, Mucha V, Styk B

机构信息

Institute of Virology, Slovak Academy of Sciences, Bratislava, Czechoslovakia.

出版信息

Arch Virol. 1988;101(1-2):13-24. doi: 10.1007/BF01314648.

DOI:10.1007/BF01314648
PMID:2458086
Abstract

Monoclonal antibodies (Mabs) specific to the HA1 and HA2 subunits of the influenza virus haemagglutinin (HA) were used to show that changes in the antigenicity of the HA molecule at acid pH involve both HA subunits. In solid phase RIA (intact virus adsorbed) the acid-induced change was detected in the form of greatly increased binding of anti-HA 1 Mabs (IVA 1 and IVG 6) and anti-HA2 Mab (IIF 4). This increased binding could be most probably explained by alterations in accessibility of epitopes to the corresponding Mabs. Other Mabs examined (including 7 anti-HA2 Mabs specific to 3 independent antigenic sites) had either similar reactivities with both untreated and pH 5-treated virus or slightly but significantly increased binding to pH 5-treated virus. No effect of pH 5 treatment on antibody binding was observed with purified BHA in solid phase RIA. Nevertheless a similar pH 5-induced conformational change in the isolated BHA (like in intact viral HA in solid phase RIA) was detected in competitive binding assay carried out in liquid phase.

摘要

针对流感病毒血凝素(HA)的HA1和HA2亚基的单克隆抗体(Mab)被用于证明,在酸性pH条件下HA分子抗原性的变化涉及两个HA亚基。在固相放射免疫分析(吸附完整病毒)中,酸诱导的变化以抗HA1 Mab(IVA 1和IVG 6)和抗HA2 Mab(IIF 4)结合大幅增加的形式被检测到。这种结合增加很可能是由于表位与相应Mab的可及性改变所致。所检测的其他Mab(包括针对3个独立抗原位点的7种抗HA2 Mab)与未处理病毒和pH 5处理病毒的反应性相似,或者与pH 5处理病毒的结合略有但显著增加。在固相放射免疫分析中,用纯化的BHA未观察到pH 5处理对抗体结合的影响。然而,在液相进行的竞争性结合试验中,检测到分离的BHA中存在类似pH 5诱导的构象变化(如固相放射免疫分析中完整病毒HA的情况)。

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Monoclonal antibodies demonstrate accessible HA2 epitopes in minor subpopulation of native influenza virus haemagglutinin molecules.单克隆抗体在天然流感病毒血凝素分子的少数亚群中显示出可及的HA2表位。
Arch Virol. 1993;130(1-2):45-56. doi: 10.1007/BF01318995.
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