Marked sequence variation between segment 4 genes of human RV-5 and simian SA 11 rotaviruses
- 1 March 1987
- journal article
- research article
- Published by Springer Nature in Archiv für die gesamte Virusforschung
- Vol. 93 (1-2) , 111-121
- https://doi.org/10.1007/bf01313897
Abstract
The complete nucleotide sequence of dsRNA gene segment 4 of a human serotype 2 rotavirus, RV-5, was determined by sequencing overlapping cloned DNA copies of the gene. Segment 4 is 2359 base pairs in length and contains a single long open reading frame of 2325 bases capable of coding for a protein of 775 amino acids, with 5′ and 3′ non coding regions of 9 and 25 nucleotides respectively. Comparison with SA 11 segment 4 sequence reveals a moderately conserved trypsin cut site and an overall amino acid homology of 69.8 percent. One localized region of 126 amino acids is only 37.8 percent homologous. Localized frame shifts account for some of this variation, but at the nucleotide level the segment 4 sequences show more variability than other rotavirus genes that have been studied so far.Keywords
This publication has 69 references indexed in Scilit:
- Clinical efficacy of the RIT 4237 live attenuated bovine rotavirus vaccine in infants vaccinated before a rotavirus epidemicThe Journal of Pediatrics, 1985
- Primary structure of the cleavage site associated with trypsin enhancement of rotavirus SA11 infectivityVirology, 1985
- Structural homologies between RNA gene segments 10 and 11 from UK bovine, simian SA11, and human Wa rotavirusesVirology, 1985
- Preparation and Characterization of Neutralizing Monoclonal Antibodies with Different Reactivity Patterns to Human RotavirusesJournal of General Virology, 1985
- Cultivation of human rotaviruses in cell cultureJournal of Medical Virology, 1984
- Gene Coding Assignments for growth Restriction, Neutralization and Subgroup Specificities of the W and DS-1 Strains of Human RotavirusJournal of General Virology, 1983
- Rotaviruses: A ReviewPublished by Springer Nature ,1983
- Proteolytic cleavage of influenza virus hemagglutinins: primary structure of the connecting peptide between HA1 and HA2 determines proteolytic cleavability and pathogenicity of avian influenza virusesVirology, 1981
- Proteolytic enhancement of rotavirus infectivity: biologic mechanismsVirology, 1980
- Ribonucleic Acid Polymerase Activity Associated with Purified Calf RotavirusJournal of General Virology, 1977