title: 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 have been deleted from a cloned gene coding for the haemagglutinin (HA) of influenza virus. The wild-type gene has previously been shown to be expressed with high efficiency from simian virus 40 (SV40)-HA recombinant 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 also is 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.
mesh_terms: D002451:Cell Compartmentation; D002872:Chromosome Deletion; D004279:DNA, Viral / Q000235:genetics; D005786:Gene Expression Regulation; D005796:Genes; D005814:Genes, Viral; D006023:Glycoproteins / Q000096:biosynthesis; D006389:Hemagglutinins, Viral / Q000235:genetics*; D009980:Influenza A virus / Q000235:genetics*; D008970:Molecular Weight; D010455:Peptides / Q000235:genetics; D021382:Protein Sorting Signals
chemical_list: D004279:DNA, Viral; D006023:Glycoproteins; D006389:Hemagglutinins, Viral; D010455:Peptides; D021382:Protein Sorting Signals