H1 and H7 influenza haemagglutinin structures extend a structural classification of heamagglutinin subtypes

Rupert James Martin Russell, SJ Gamblin, LF Haire, DJ Stevens, B Xiao, Y Ha, JJ Skehel

Research output: Contribution to journalArticlepeer-review

160 Citations (Scopus)

Abstract

Comparing the structures of H3, H5 and H9 subtype haemagglutinins, we deduced a structural basis for including all 15 influenza subtypes in four clades. H3, H5 and H9 represent three of these clades; we now report the structure of an H7 HA as a representative of the fourth clade. We confirm the structure of the turn at the N-terminus of the conserved central alpha-helix of HA2, and the combination of ionisable residues near the "fusion peptide" as clade-specific features. We compare the structures of three H1 HAs with H5 HA in the same clade, to refine our previous classification and we confirm the division of the clades into two groups of two. We also show the roles of carbohydrate side chains in the esterase-fusion domain boundaries in the formation of clade-specific structural markers. (C) 2004 Elsevier Inc. All rights reserved.

Original languageEnglish
Pages (from-to)287-296
Number of pages10
JournalVirology
Volume325
Issue number2
DOIs
Publication statusPublished - 1 Aug 2004

Keywords

  • H1
  • H7
  • influenza
  • haemagglutinin
  • RECEPTOR-BINDING PROPERTIES
  • MEMBRANE-FUSION
  • VIRUS
  • PH
  • GLYCOPROTEIN
  • MUTANTS
  • ORIGIN

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