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流感 H5N1 病毒血凝素的抗原结构。

The antigenic architecture of the hemagglutinin of influenza H5N1 viruses.

机构信息

Drug Delivery, Disposition and Dynamics, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, Victoria 3052, Australia.

出版信息

Mol Immunol. 2013 Dec;56(4):705-19. doi: 10.1016/j.molimm.2013.07.010. Epub 2013 Aug 7.

DOI:10.1016/j.molimm.2013.07.010
PMID:23933511
Abstract

Human infection with the highly pathogenic avian influenza A virus H5N1 is associated with a high mortality and morbidity. H5N1 continues to transmit from poultry to the human population, raising serious concerns about its pandemic potential. Current influenza H5N1 vaccines are based upon the elicitation of a neutralizing antibody (Ab) response against the major epitope regions of the viral surface glycoprotein, hemagglutinin (HA). However, antigenic drift mutations in immune-dominant regions on the HA structure allow the virus to escape Ab neutralization. Epitope mapping using neutralizing monoclonal antibodies (mAb) helps define mechanisms of antigenic drift, neutralizing escape and can facilitate pre-pandemic vaccine design. This review explores the current knowledge base of the antigenic sites of the H5N1 HA molecule. The relationship between the epitope architecture of the H5N1 HA, antigenic evolution of the different H5N1 lineages and the antigenic complexity of the H5N1 virus lineages that constitute potential pandemic strains are discussed in detail.

摘要

人感染高致病性禽流感病毒 H5N1 与高死亡率和发病率有关。H5N1 继续从禽类传播到人群,引发了人们对其大流行潜力的严重关注。目前的流感 H5N1 疫苗是基于对病毒表面糖蛋白血凝素 (HA) 的主要表位区域产生中和抗体 (Ab) 反应。然而,HA 结构上免疫优势区域的抗原漂移突变允许病毒逃避 Ab 中和。使用中和单克隆抗体 (mAb) 进行表位作图有助于确定抗原漂移、中和逃逸的机制,并可以促进大流行前疫苗设计。本文综述了 H5N1 HA 分子抗原表位的现有知识库。详细讨论了 H5N1 HA 的表位结构、不同 H5N1 谱系的抗原进化以及构成潜在大流行株的 H5N1 病毒谱系的抗原复杂性之间的关系。

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