Cell-surface expression of influenza haemagglutinin from a cloned DNA copy of the RNA gene
- 1 October 1981
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 293 (5834) , 620-625
- https://doi.org/10.1038/293620a0
Abstract
By replacing either the early or the late genes of SV40 with a cloned copy of the influenza virus haemagglutinin gene we have constructed recombinant viruses which, in infected cells, express large quantities of haemagglutinin. This glycoprotein, over 108 molecules of which are produced per cell, is identical in molecular weight to authentic influenza virus haemagglutinin, accumulates at the cell surface and displays haemabsorbing activity.This publication has 53 references indexed in Scilit:
- Primary structure of a murine transplantation antigenNature, 1981
- Rat brain Thy-1 glycoprotein. The amino acid sequence, disulphide bonds and an unusual hydrophobic regionBiochemical Journal, 1981
- The Amino Acid Sequence of a Hong Kong Influenza Haemagglutinin Light (HA2) ChainJournal of General Virology, 1980
- Cloning and DNA sequence of double-stranded copies of haemagglutinin genes from H2 and H3 strains elucidates antigenic shift and drift in human influenza virusNature, 1980
- Completion of the amino acid sequence of a Hong Kong influenza hemagglutinin heavy chain: Sequence of cyanogen bromide fragment CN1Virology, 1980
- Complete structure of the hemagglutinin gene from the human influenza A/Victoria/3/75 (H3N2) strain as determined from cloned DNACell, 1980
- Complete nucleotide suquence of the haemagglutinin gene from a human influenza virus of the Hong Kong subtypeNucleic Acids Research, 1980
- Complete nucleotide sequence of an influenza virus haemagglutinin gene from cloned DNANature, 1979
- Comparison of amino acid sequences of two human histocompatibility antigens, HLA-A2 and HLA-B7: location of putative alloantigenic sites.Proceedings of the National Academy of Sciences, 1979
- Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin.Proceedings of the National Academy of Sciences, 1975