Mutational Analysis of the Structure and Function of the Influenza Virus Hemagglutinin

Mary Jane Gething, Carolyn Doyle, Michael Roth, Joe Sambrook

Research output: Contribution to journalArticlepeer-review

4 Scopus citations


Hemagglutinin (HA) glycoprotein of influenza virus is considered the best characterized of all integral membrane proteins. HA is regarded as an ideal candidate for site-specific mutagenesis experiments aimed at elucidating the function of the various domains of the molecule. The structure of the HA molecule is characteristic of the major class of cellular integral membrane proteins, having typical amino and carboxy-terminal hydrophobic regions. Essentially, HA provides a useful model system for the study of the structure, function, and biosynthesis of eukaryotic membrane proteins. The HA protein is naturally encoded by an RNA genome that is not amenable to in vitro mutagenesis. When the HA cDNA is introduced into eukaryotic cells using vectors derived from SV40, it is expressed with high efficiency into a fully glycosylated protein that is displayed on the infected cell's surface in an antigenically and biologically active form. The cloned, expressing copies of the HA gene provide the material to analyze the effect of mutations on the structure and function of the protein. This chapter presents the expression of wild-type HA and analysis of the expression of mutant HA proteins.

Original languageEnglish (US)
Pages (from-to)17-41
Number of pages25
JournalCurrent Topics in Membranes and Transport
Issue numberC
StatePublished - Jan 1 1985

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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