Preferential Recognition of Avian-Like Receptors in Human Influenza A H7N9 Viruses

被引：126

作者：

Xu, Rui ^{[1
]}

de Vries, Robert P. ^{[2
,3
]}

Zhu, Xueyong ^{[1
]}

Nycholat, Corwin M. ^{[2
,3
]}

McBride, Ryan ^{[2
,3
]}

Yu, Wenli ^{[1
]}

Paulson, James C. ^{[2
,3
]}

Wilson, Ian A. ^{[1
,4
]}

机构：

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

[2] Scripps Res Inst, Dept Cell & Mol Biol, La Jolla, CA 92037 USA

[3] Scripps Res Inst, Dept Physiol Chem, La Jolla, CA 92037 USA

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

来源：

SCIENCE | 2013年 / 342卷 / 6163期

关键词：

HUMAN INFECTION; BINDING; TRANSMISSION; SPECIFICITY; HEMAGGLUTININS; FERRETS; DETERMINANT; COMPLEXES; ORIGIN; ACID;

D O I：

10.1126/science.1243761

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The 2013 outbreak of avian-origin H7N9 influenza in eastern China has raised concerns about its ability to transmit in the human population. The hemagglutinin glycoprotein of most human H7N9 viruses carries Leu(226), a residue linked to adaptation of H2N2 and H3N2 pandemic viruses to human receptors. However, glycan array analysis of the H7 hemagglutinin reveals negligible binding to humanlike alpha 2-6-linked receptors and strong preference for a subset of avian-like alpha 2-3-linked glycans recognized by all avian H7 viruses. Crystal structures of H7N9 hemagglutinin and six hemagglutinin-glycan complexes have elucidated the structural basis for preferential recognition of avian-like receptors. These findings suggest that the current human H7N9 viruses are poorly adapted for efficient human-to-human transmission.

引用

页码：1230 / 1235

页数：6

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