Structural insights into the design of novel anti-influenza therapies

被引:74
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
关键词
INFLUENZA-A VIRUS; RECEPTOR-BINDING PROPERTIES; ANTIBODY RECOGNITION; HEMAGGLUTININ-STEM; CONFORMATIONAL-CHANGE; COMPUTATIONAL DESIGN; NEUTRALIZING EPITOPE; PROTECTS MICE; SPECIFICITY; SITE;
D O I
10.1038/s41594-018-0025-9
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A limited arsenal of therapies is currently available to tackle the emergence of a future influenza pandemic or even to deal effectively with the continual outbreaks of seasonal influenza. However, recent findings hold great promise for the design of novel vaccines and therapeutics, including the possibility of more universal treatments. Structural biology has been a major contributor to those advances, in particular through the many studies on influenza hemagglutinin (HA), the major surface antigen. HA's primary function is to enable the virus to enter host cells, and structural work has revealed the various HA conformational forms generated during the entry process. Other studies have explored how human broadly neutralizing antibodies (bnAbs), designed proteins, peptides and small molecules, can inhibit and neutralize the virus. Here we review milestones in HA structural biology and how the recent insights from bnAbs are paving the way to design novel vaccines and therapeutics.
引用
收藏
页码:115 / 121
页数:7
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