Identification of the Rubella Virus Nonstructural Proteins
نویسندگان
چکیده
منابع مشابه
Identification of a Ca2+-binding domain in the rubella virus nonstructural protease.
The rubella virus (RUB) nonstructural protein (NS) open reading frame (ORF) encodes a polypeptide precursor that is proteolytically self cleaved into two replicase components involved in viral RNA replication. A putative EF-hand Ca(2+)-binding motif that was conserved across different genotypes of RUB was predicted within the nonstructural protease that cleaves the precursor by using bioinforma...
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Immunoprecipitation of [3H]amino acid labelled virus with monoclonal or human convalescent rubella sera and subsequent analysis by electrophoresis and fluorography, revealed three structural proteins of rubella virus: VP3: 59,000; VP2: 44,800; and VP1: 33,000.
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The full-length nonstructural protein P90 of rubella virus (RV) was expressed as recombinant protein in Escherichia coli bacteria, as well as in Vero cells. Monoclonal antibodies raised against the protein specifically reacted with the protein in both P90-transfected and RV infected Vero cells. Ninety human sera obtained from reconvalescents, vaccinees and patients with acute RV infection were ...
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5 ACKNOWLEDGEMENTS 6 ORIGINAL PUBLICATIONS 7 ABBREVIATIONS 8
متن کاملCharacterization of the zinc binding activity of the rubella virus nonstructural protease.
The rubella virus (RUB) nonstructural (NS) protein (NSP) ORF encodes a protease that cleaves the NSP precursor (240 kDa) at a single site to produce two products. A cleavage site mutation was introduced into a RUB infectious cDNA clone and found to be lethal, demonstrating that cleavage of the NSP precursor is necessary for RUB replication. Based on computer alignments, the RUB NS protease was ...
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ژورنال
عنوان ژورنال: Virology
سال: 1995
ISSN: 0042-6822
DOI: 10.1006/viro.1995.1007