VP7 serotype-specific glycoprotein of OSU porcine rotavirus: coding assignment and gene sequence

1 Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, U.S.A. 2 Instituto Venezolano de Investigaciones Cientificas, Laboratorio de Biologia de Virus, Apartado 1827, Caracas 1010A, Venezuela and 3 Laborator...

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Veröffentlicht in:Journal of general virology 1986-11, Vol.67 (11), p.2445-1454
Hauptverfasser: Gorziglia, M, Aguirre, Y, Hoshino, Y, Esparza, J, Blumentals, I, Askaa, J, Thompson, M, Glass, R.I, Kapikian, A.Z, Chanock, R.M
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Sprache:eng
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Zusammenfassung:1 Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, U.S.A. 2 Instituto Venezolano de Investigaciones Cientificas, Laboratorio de Biologia de Virus, Apartado 1827, Caracas 1010A, Venezuela and 3 Laboratory of Molecular and Developmental Biology, National Eye Institute, National Institutes of Health, Bethesda, Maryland 20892, U.S.A. With a reassortant from a cross of human rotavirus DS-1 (serotype 2) and OSU (serotype 5) it was determined that the OSU major neutralization glycoprotein antigen (VP7) was encoded by gene segment 9. A full-sized cloned cDNA copy of the OSU gene 9 was produced and sequenced. Hybridization of such labelled cDNA with the corresponding segment of a reassortant DS-1 x OSU virus confirmed the coding assignment. Comparison of the deduced amino acid sequence of the VP7 of OSU with those previously determined for five other rotavirus strains, representing four distinct serotypes, revealed some hydrophilic regions that exhibited significant homology and other hydrophilic domains with greater amino acid divergence. In one of the latter hydrophilic domains each of the five serotypes had a distinct amino acid substitution at residue 146, suggesting that it may be involved in serotype specificity. Keywords: rotavirus (porcine) gene 9, sequencing, coding assignment of VP7 Present address: Department of Chemical Engineering, The Johns Hopkins University, Baltimore, Maryland 21218, U.S.A. Present address: Dakopatts, 42, Produktionsved, P.O. Box 1359, DK-2600 Glostrup, Denmark. Received 17 February 1986; accepted 9 July 1986.
ISSN:0022-1317
1465-2099
DOI:10.1099/0022-1317-67-11-2445