Structural insights into the design of novel anti-influenza therapies

Nat Struct Mol Biol. 2018 Feb;25(2):115-121. doi: 10.1038/s41594-018-0025-9. Epub 2018 Feb 2.


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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Antibodies, Neutralizing / immunology
  • Antibodies, Viral / immunology
  • Antiviral Agents / chemistry
  • Binding Sites
  • Crystallography, X-Ray
  • Ferrets
  • Haplorhini
  • Hemagglutinin Glycoproteins, Influenza Virus / chemistry*
  • Humans
  • Hydroquinones / chemistry
  • Influenza Vaccines / therapeutic use*
  • Influenza, Human / prevention & control*
  • Influenza, Human / therapy
  • Kinetics
  • Mice
  • Models, Molecular
  • Peptides / chemistry
  • Protein Multimerization


  • Antibodies, Neutralizing
  • Antibodies, Viral
  • Antiviral Agents
  • Hemagglutinin Glycoproteins, Influenza Virus
  • Hydroquinones
  • Influenza Vaccines
  • Peptides
  • 2-tert-butylhydroquinone