Construction of influenza haemagglutinin genes that code for intracellular and secreted forms of the protein

Abstract

The DNA sequences encoding the amino-terminal signal peptide or the carboxy-terminal hydrophobic anchor were deleted from a cloned gene coding for the hemagglutinin (HA) of influenza virus. The wild-type gene was previously shown to be expressed with high efficiency from SV40-HA recomnbinant vectors into a fully glycosylated protein that is displayed on the infected cell''s surface in an antigenically and biologically active form. The anchor-minus HA is also glycosylated but is secreted efficiently into the medium. By contrast, the signal-minus HA is produced only at low levels, is not glycosylated and is located intracellularly.