Influenza Hemagglutinin Structures and Antibody Recognition

被引：153

作者：

Wu, Nicholas C. ^{[1
]}

Wilson, Ian A. ^{[1
,2
]}

机构：

[1] Scripps Res Inst, Dept Integrat Struct & Computat Biol, La Jolla, CA 92037 USA

[2] Scripps Res Inst, Skaggs Inst Chem Biol, La Jolla, CA 92037 USA

来源：

COLD SPRING HARBOR PERSPECTIVES IN MEDICINE | 2020年 / 10卷 / 08期

关键词：

RECEPTOR-BINDING SITE; BROADLY NEUTRALIZING ANTIBODIES; HUMAN MONOCLONAL-ANTIBODIES; AMINO-ACID SUBSTITUTIONS; N-LINKED GLYCOSYLATION; VIRUS HEMAGGLUTININ; A VIRUSES; ANTIGENIC STRUCTURE; GLOBULAR HEAD; IN-VIVO;

D O I：

10.1101/cshperspect.a038778

中图分类号：

R-3 [医学研究方法]; R3 [基础医学];

学科分类号：

1001 ;

摘要：

Hemagglutinin (HA) is most abundant glycoprotein on the influenza virus surface. Influenza HA promotes viral entry by engaging the receptor and mediating virus-host membrane fusion. At the same time, HA is the major antigen of the influenza virus. HA antigenic shift can result in pandemics, whereas antigenic drift allows human circulating strains to escape herd immunity. Most antibody responses against HA are strain-specific. However, antibodies that have neutralizing activities against multiple strains or even subtypes have now been discovered and characterized. These broadly neutralizing antibodies (bnAbs) target conserved regions on HA, such as the receptor-binding site and the stem domain. Structural studies of such bnAbs have provided important insight into universal influenza vaccine and therapeutic design. This review discusses the HA functions as well as HA antibody interactions from a structural perspective.

引用

页码：1 / 20

页数：20

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