Nucleotide sequence of the Bunyamwera virus M RNA segment: Conservation of structural features in the Bunyavirus glycoprotein gene product
Identifieur interne : 002357 ( Main/Exploration ); précédent : 002356; suivant : 002358Nucleotide sequence of the Bunyamwera virus M RNA segment: Conservation of structural features in the Bunyavirus glycoprotein gene product
Auteurs : Janice F. Lees [Royaume-Uni] ; Craig R. Pringle [Royaume-Uni] ; Richard M. Elliott [Royaume-Uni]Source :
- Virology [ 0042-6822 ] ; 1986.
English descriptors
- Teeft :
- Academic press, Akashi, Amino, Amino acid sequences, Amino acids, Bunyamwera, Bunyamwera cells, Bunyamwera virus, Bunyavirus, Bunyavirus genus, Cdna, Cdna clones, Cleavage, Clone, Codon, Consensus sequence, Crosse, Crosse virus, Cysteine, Cysteine residues, Eshita, Family bunyaviridae, Gene product, Gene products, Genome, Glycoprotein, Hare, Homol program, Homology, Lees, Mature proteins, Molecular weight, Nonstructural protein, Nucleic, Nucleic acids, Nucleotide, Nucleotide sequence, Nucleotide sequences, Plasmid, Polyprotein, Potential glycosylation sites, Precursor, Pringle, Rna, Sequence information, Signal sequence, Snowshoe, Snowshoe hare, Snowshoe hare bunyavirus, Snowshoe hare virus, Terminus, Tunicamycin, Unpublished data, Viral, Virology, Virus.
Abstract
Abstract: The complete nucleotide sequence of the Bunyamwera virus M RNA segment was determined from four overlapping cDNA clones and by primer extension. The RNA segment is 4458 bases in length, and encodes a single gene product in the viral complementary RNA. The predicted protein is 1433 amino acids long (mol wt 162,065), contains four potential glycosylation sites, and is relatively cysteine rich. It is presumed that the three proteins G1, G2, and NSM which have been mapped to the M RNA segment are synthesized as a precursor polyprotein which is subsequently proteolytically cleaved. A putative hydrophobic signal sequence at the amino terminus and a hydrophobic anchor sequence at the carboxy terminus of the predicted protein have been identified, in addition to internal regions of hydrophobicity of unknown function. The nucleotide and amino acid sequences of the Bunyamwera virus M segment have been compared with those of the snowshoe hare virus M segment (Y. Eshita and D. H. L. Bishop, Virology 137,227–240, 1984). Common features include the overall architecture of the RNAs, single cysteine-rich primary gene products, and conservation of hydrophobic domains in the gene products. When aligned the amino acid sequences are 43% homologous, and 66 of 70 cysteine residues can be matched. The evolutionary significance of these findings is discussed.
Url:
DOI: 10.1016/0042-6822(86)90398-3
Affiliations:
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<front><div type="abstract" xml:lang="en">Abstract: The complete nucleotide sequence of the Bunyamwera virus M RNA segment was determined from four overlapping cDNA clones and by primer extension. The RNA segment is 4458 bases in length, and encodes a single gene product in the viral complementary RNA. The predicted protein is 1433 amino acids long (mol wt 162,065), contains four potential glycosylation sites, and is relatively cysteine rich. It is presumed that the three proteins G1, G2, and NSM which have been mapped to the M RNA segment are synthesized as a precursor polyprotein which is subsequently proteolytically cleaved. A putative hydrophobic signal sequence at the amino terminus and a hydrophobic anchor sequence at the carboxy terminus of the predicted protein have been identified, in addition to internal regions of hydrophobicity of unknown function. The nucleotide and amino acid sequences of the Bunyamwera virus M segment have been compared with those of the snowshoe hare virus M segment (Y. Eshita and D. H. L. Bishop, Virology 137,227–240, 1984). Common features include the overall architecture of the RNAs, single cysteine-rich primary gene products, and conservation of hydrophobic domains in the gene products. When aligned the amino acid sequences are 43% homologous, and 66 of 70 cysteine residues can be matched. The evolutionary significance of these findings is discussed.</div>
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