Structural insights into the design of novel anti-influenza therapies

被引:0
作者
Nicholas C. Wu
Ian A. Wilson
机构
[1] The Scripps Research Institute,Department of Integrative Structural and Computational Biology
[2] The Scripps Research Institute,The Skaggs Institute for Chemical Biology
来源
Nature Structural & Molecular Biology | 2018年 / 25卷
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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.
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页码:115 / 121
页数:6
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  • [1] Jefferson T(2014)Neuraminidase inhibitors for preventing and treating influenza in healthy adults and children Cochrane Database Syst. Rev. 4 CD008965-4274
  • [2] Tong S(2012)A distinct lineage of influenza A virus from bats Proc. Natl. Acad. Sci. USA 109 4269-373
  • [3] Tong S(2013)New world bats harbor diverse influenza A viruses PLoS Pathog. 9 366-378
  • [4] Wilson IA(1981)Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution Nature 289 373-78
  • [5] Skehel JJ(1981)Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation Nature 289 76-431
  • [6] Wiley DC(1983)Single amino acid substitutions in influenza haemagglutinin change receptor binding specificity Nature 304 426-417
  • [7] Wiley DC(1988)Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid Nature 333 409-18261
  • [8] Wilson IA(1998)Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation Cell 95 18256-1265
  • [9] Skehel JJ(2013)Cleavage strongly influences whether soluble HIV-1 envelope glycoprotein trimers adopt a native-like conformation Proc. Natl. Acad. Sci. USA 110 1262-1870
  • [10] Rogers GN(1994)Crystals of a fragment of influenza haemagglutinin in the low pH induced conformation J. Mol. Biol. 236 1866-1842