The structure and receptor binding properties of the 1918 Influenza Hemagglutinin

SJ Gamblin, LF Haire, Rupert James Martin Russell, DJ Stevens, B Xiao, Y Ha, N Vasisht, DA Steinhauer, RS Daniels, A Elliot, DC Wiley, JJ Skehel

Research output: Contribution to journalArticlepeer-review

609 Citations (Scopus)

Abstract

The 1918 influenza pandemic resulted in about 20 million deaths. This enormous impact, coupled with renewed interest in emerging infections, makes characterization of the virus involved a priority. Receptor binding, the initial event in virus infection, is a major determinant of virus transmissibility that, for influenza viruses, is mediated by the hemagglutinin ( HA) membrane glycoprotein. We have determined the crystal structures of the HA from the 1918 virus and two closely related HAs in complex with receptor analogs. They explain how the 1918 HA, while retaining receptor binding site amino acids characteristic of an avian precursor HA, is able to bind human receptors and how, as a consequence, the virus was able to spread in the human population.

Original languageEnglish
Pages (from-to)1838-1842
Number of pages5
JournalScience
Volume303
Issue number5665
DOIs
Publication statusPublished - 19 Mar 2004

Keywords

  • VIRUS HEMAGGLUTININS
  • SPANISH INFLUENZA
  • SIALIC-ACID
  • A-VIRUSES
  • SPECIFICITY
  • ORIGIN
  • H1
  • EVOLUTION
  • VARIANTS
  • CELL

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