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Nucleotide Sequences of the MRNA's Encoding the Vesicular Stomatitis Virus G and M Proteins Determined from CDNA Clones Containing the Complete Coding Regions

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Journal J Virol
Date 1981 Aug 1
PMID 6268840
Citations 189
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Abstract

The complete nucleotide sequences of the vesicular stomatitis virus mRNA's encoding the glycoprotein (G) and the matrix protein (M) have been determined from cDNA clones that contain the complete coding sequences from each mRNA. The G protein mRNA is 1,665 nucleotides long, excluding polyadenylic acid, and encodes a protein of 511 amino acids including a signal peptide of 16 amino acids. G protein contains two large hydrophobic domains, one in the signal peptide and the other in the transmembrane segment near the COOH terminus. Two sites of glycosylation are predicted at amino acid residues 178 and 335. The close correspondence of the positions of these sites with the reported timing of the addition of the two oligosaccharides during synthesis of G suggests that glycosylation occurs as soon as the appropriate asparagine residues traverse the membrane of the rough endoplasmic reticulum. The mRNA encoding the vesicular stomatitis virus M protein is 831 nucleotides long, excluding polyadenylic acid, and encodes a protein of 229 amino acids. The predicted M protein sequence does not contain any long hydrophobic or nonpolar domains that might promote membrane association. The protein is rich in basic amino acids and contains a highly basic amino terminal domain. Details of construction of the nearly full-length cDNA clones are presented.

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References
1.
Cartwright B, Smale C, Brown F . Surface structure of vesicular stomatitis virus. J Gen Virol. 1969; 5(1):1-10. DOI: 10.1099/0022-1317-5-1-1. View

2.
Cohen G, Atkinson P, Summers D . Interactions of vesicular stomatitis virus structural proteins with HeLa plasma membranes. Nat New Biol. 1971; 231(21):121-3. DOI: 10.1038/newbio231121a0. View

3.
Wensink P, Finnegan D, Donelson J, Hogness D . A system for mapping DNA sequences in the chromosomes of Drosophila melanogaster. Cell. 1974; 3(4):315-25. DOI: 10.1016/0092-8674(74)90045-2. View

4.
Bishop D, Repik P, Obijeski J, Moore N, Wagner R . Restitution of infectivity to spikeless vesicular stomatitis virus by solubilized viral components. J Virol. 1975; 16(1):75-84. PMC: 354634. DOI: 10.1128/JVI.16.1.75-84.1975. View

5.
Morrison T . Site of synthesis of membrane and nonmembrane proteins of vesicular stomatitis virus. J Biol Chem. 1975; 250(17):6955-62. View