reviewJournal of Biological ChemistryJun 11, 2010HYBRID OA

Influenza Hemagglutinin and Neuraminidase Membrane Glycoproteins

National Institute for Medical Research · Medical Research Council · +1 more institution

PubMed
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Abstract

Considerable progress has been made toward understanding the structural basis of the interaction of the two major surface glycoproteins of influenza A virus with their common ligand/substrate: carbohydrate chains terminating in sialic acid. The specificity of virus attachment to target cells is mediated by hemagglutinin, which acquires characteristic changes in its receptor-binding site to switch its host from avian species to humans. Anti-influenza drugs mimic the natural sialic acid substrate of the virus neuraminidase enzyme but utilize the much tighter binding of the drugs for efficacy. Resistance to one of the two main antiviral drugs is differentially acquired by the two distinct subsets of neuraminidase…

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629
total citations
FWCI
22.56
Percentile
100%
References
98
Citations per year

Authors

2

Topics & keywords

Keywords
  • Neuraminidase
  • Sialic acid
  • Glycoprotein
  • Hemagglutinin (influenza)
  • Virus
  • Enzyme
  • Biology
  • Neuraminic acid
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