Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain

Peter Scheiffele, Michael G. Roth, Kai Simons

Research output: Contribution to journalArticle

553 Scopus citations

Abstract

Sphingolipid-cholesterol rafts are microdomains in biological membranes with liquid-ordered phase properties which are implicated in membrane traffic and signalling events. We have used influenza virus haemagglutinin (HA) as a model protein to analyse the interaction of transmembrane proteins with these microdomains. Here we demonstrate that raft association is an intrinsic property encoded in the protein. Mutant HA molecules with foreign transmembrane domain (TMD) sequences lose their ability to associate with the lipid microdomains, and mutations in the HA TMD reveal a requirement for hydrophobic residues in contact with the exoplasmic leaflet of the membrane. We also provide experimental evidence that cholesterol is critically required for association of proteins with lipid rafts. Our data suggest that the binding to specific membrane domains can be encoded in transmembrane proteins and that this information will be used for polarized sorting and signal transduction processes.

Original languageEnglish (US)
Pages (from-to)5501-5508
Number of pages8
JournalEMBO Journal
Volume16
Issue number18
DOIs
StatePublished - Sep 15 1997

Keywords

  • Cholesterol
  • Microdomain
  • Polarized sorting
  • Signal transduction
  • Transmembrane domain

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

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