| Literature DB >> 12127789 |
Elida M Bautista1, Kay S Faaberg, Dan Mickelson, Edward D McGruder.
Abstract
Porcine reproductive and respiratory syndrome virus (PRRSV) is a member of the positive-strand RNA virus family Arteriviridae. Although considerable research has focused on this important pathogen, little is known about the function of most PRRSV proteins. To examine characteristics of putative nonstructural proteins (nsp) encoded in ORF1b, which have been identified by nucleotide similarity to domains of equine arteritis virus, defined genomic regions were cloned and expressed in the pRSET expression system. One region, nsp10, encoded a protein with a putative helicase domain and was further examined for functional helicase-like activities. PRRSV nsp10 was found to possess a thermolabile and pH-sensitive NTPase activity that was modulated by polynucleotides and to unwind dsRNA in a 5' to 3' polarity. These results provide the first evidence of the functional properties of PRRSV helicase and further support the finding that nidovirus helicases possess properties that distinguish them from other viral helicases.Entities:
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Year: 2002 PMID: 12127789 PMCID: PMC7130902 DOI: 10.1006/viro.2002.1495
Source DB: PubMed Journal: Virology ISSN: 0042-6822 Impact factor: 3.616