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利用血凝素蛋白的合成肽分析对麻疹病毒的中和抗体反应。

Analysis of the neutralizing antibody response to the measles virus using synthetic peptides of the haemagglutinin protein.

作者信息

Muller C P, Schroeder T, Tu R, Brons N H, Jung G, Schneider F, Wiesmüller K H

机构信息

Laboratoire National de Santé, Luxembourg.

出版信息

Scand J Immunol. 1993 Nov;38(5):463-71. doi: 10.1111/j.1365-3083.1993.tb02589.x.

DOI:10.1111/j.1365-3083.1993.tb02589.x
PMID:7694357
Abstract

Infection or immunization with measles virus induces a protective immune reaction including neutralizing antibodies against the haemagglutinin and fusion protein. The reactivity of the polyclonal IgG response of sera obtained from late convalescent donors was studied, using overlapping 15mer peptides covering the complete sequence of the measles virus haemagglutinin. Most sera reacted with a similar set of peptides generating a characteristic binding pattern. The reactive peptides correspond to a region mediating cell hemolysis (aa310-325), to regions which serve as targets to neutralizing antibodies and to a putative transmembrane region (aa35-58). The latter region contains also a human T-cell epitope providing evidence of a non-random association of T- and B-cell epitopes. We also immunized different strains of mice and rabbits with measles virus. In contrast to the human sera, animal sera with strong neutralizing activities did not react with any of the H-protein peptides. The mostly weak reactivities with the linear sequences contrast with the strong neutralizing activities of the human or animal antibodies, suggesting that these primarily recognize the fusion protein or conformational epitopes of the haemagglutinin protein.

摘要

感染麻疹病毒或进行麻疹病毒免疫接种会引发一种保护性免疫反应,包括产生针对血凝素和融合蛋白的中和抗体。利用覆盖麻疹病毒血凝素完整序列的重叠15聚体肽,研究了从恢复期晚期供体获得的血清中多克隆IgG反应的反应性。大多数血清与一组相似的肽发生反应,产生一种特征性的结合模式。反应性肽对应于介导细胞溶血的区域(氨基酸310 - 325)、作为中和抗体靶点的区域以及一个推定的跨膜区域(氨基酸35 - 58)。后一个区域还包含一个人类T细胞表位,这为T细胞和B细胞表位的非随机关联提供了证据。我们还用麻疹病毒免疫了不同品系的小鼠和兔子。与人类血清不同,具有强中和活性的动物血清与任何H蛋白肽均无反应。与人类或动物抗体的强中和活性相比,动物血清与线性序列的反应大多较弱,这表明这些抗体主要识别融合蛋白或血凝素蛋白的构象表位。

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