Glycan Receptor Binding of the Influenza A Virus H7N9 Hemagglutinin

被引：160

作者：

Tharakaraman, Kannan ^{[1
]}

Jayaraman, Akila ^{[1
]}

Raman, Rahul ^{[1
]}

Viswanathan, Karthik ^{[1
]}

Stebbins, Nathan W. ^{[1
]}

Johnson, David ^{[1
]}

Shriver, Zachary ^{[1
]}

Sasisekharan, V. ^{[1
]}

Sasisekharan, Ram ^{[1
]}

机构：

[1] MIT, Singapore MIT Alliance Res & Technol, Dept Biol Engn,Koch Inst Integrat Canc Res, Infect Dis Interdisciplinary Res Grp, Cambridge, MA 02139 USA

来源：

CELL | 2013年 / 153卷 / 07期

基金：

美国国家卫生研究院;

关键词：

RESPIRATORY-TRACT; TRANSMISSION; HA; PATHOGENESIS; ADAPTATION; SITES;

D O I：

10.1016/j.cell.2013.05.034

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

The advent of H7N9 in early 2013 is of concern for a number of reasons, including its capability to infect humans, the lack of clarity in the etiology of infection, and because the human population does not have pre-existing immunity to the H7 subtype. Earlier sequence analyses of H7N9 hemagglutinin (HA) point to amino acid changes that predicted human receptor binding and impinge on the antigenic characteristics of the HA. Here, we report that the H7N9 HA shows limited binding to human receptors; however, should a single amino acid mutation occur, this would result in structural changes within the receptor binding site that allow for extensive binding to human receptors present in the upper respiratory tract. Furthermore, a subset of the H7N9 HA sequences demarcating coevolving amino acids appears to be in the antigenic regions of H7, which, in turn, could impact effectiveness of the current WHO-recommended prepandemic H7 vaccines.

引用

页码：1486 / 1493

页数：8

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