By Felix Bronner and Arnost Kleinzeller (Eds.)
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Extra resources for Genes and Membranes: Transport Proteins and Receptors
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A. (1983). The influenza virus RNA segments and their encoded proteins. In “Genetics of Influenza Viruses” (P. Palese and D. W. ), pp. 21-69. Springer-Verlag, Berlin and New York. Lodish, F. , Kong, N . , Snider, M.. and Strous, G . J. A. M. (1983). Hepatoma secretory proteins migrate from the rough endoplasmic reticulum to the Golgi at characteristic rates. Nature (London) 304, 80-83. McCutchan, J. , and Pagano, J . S . (1968). Enhancement of the infectivity of simian virus 40 deoxyribonucleic acid with diethyl aminoethyl-dextran.
Linear map of HA from the A/Japan/305/57 strain of influenza virus. The map relates the various functional regions of the molecule to the restriction sites in the gene. sequence; H,glycosylation site; 0, antigenic site. A. Deletion of the Signal Sequence Converts HA to a Nonglycosylated, lntracellular Protein The double-stranded exonuclease Ba131 was used to remove from the wildtype HA sequences the 5' nucleotides coding for the N-terminal signal peptide. The truncated gene was used to replace the wild-type gene in the SV40-HA vector, so that the HA initiation codon was fused in frame to the codon for the first amino acid of the mature HA polypeptide, leaving unaltered the remainder of the coding sequences (Gething and Sambrook, 1982).
The infective entry of influenza virus into MDCK cells. J . Cell Biol. 91, 601-613. , Marshall, R . , and Spiro, R. G. (1972). “The Glycoproteins: Their Composition, Structure and Functions,” pp. 450-490. Elsevier, Amsterdam. Pipas. J. M . , Adler, S . P . , Peden, K. W. C . , and Nathans, D. (1979). Deletion mutants of SV40 that affect the structure of viral tumor antigens. Cold Spring Harbor Symp. Quanr. Biol. 44, 285291. Richardson, C. , and Choppin, P. W. (1980). Specific inhibition of paramyxovirus and myxovirus replication with oligopeptides with amino acid sequences similar to those at the N-termini of the F , or HA, viral polypeptides.