Functional properties of the predicted helicase of porcine reproductive and respiratory syndrome virus

被引:104
作者
Bautista, EM
Faaberg, KS
Mickelson, D
McGruder, ED
机构
[1] Eli Lilly & Co, Elanco Anim Hlth Res & Dev Div, Greenfield, IN 46140 USA
[2] Univ Minnesota, Dept Vet Pathobiol, St Paul, MN 55108 USA
关键词
PRRSV; arterivirus; coronavirus; Nidovirales; RNA-dependent RNA polymerase; helicase; NTPase;
D O I
10.1006/viro.2002.1495
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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 nuclectide 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. (C) 2002 Elsevier science (USA).
引用
收藏
页码:258 / 270
页数:13
相关论文
共 60 条
[31]   COMPARISON OF THE STRUCTURAL PROTEIN-CODING SEQUENCES OF THE VR-2332 AND LELYSTAD VIRUS-STRAINS OF THE PRRS VIRUS [J].
MURTAUGH, MP ;
ELAM, MR ;
KAKACH, LT .
ARCHIVES OF VIROLOGY, 1995, 140 (08) :1451-1460
[32]   Porcine reproductive and respiratory syndrome virus comparison: Divergent evolution on two continents [J].
Nelsen, CJ ;
Murtaugh, MP ;
Faaberg, KS .
JOURNAL OF VIROLOGY, 1999, 73 (01) :270-280
[33]   Analysis of ORF 1 in European porcine reproductive and respiratory syndrome virus by long RT-PCR and restriction fragment length polymorphism (RFLP) analysis [J].
Nielsen, HS ;
Storgaard, T ;
Oleksiewicz, MB .
VETERINARY MICROBIOLOGY, 2000, 76 (03) :221-228
[34]   LACTATE DEHYDROGENASE-ELEVATING VIRUS, EQUINE ARTERITIS VIRUS, AND SIMIAN HEMORRHAGIC-FEVER VIRUS - A NEW GROUP OF POSITIVE-STRAND RNA VIRUSES [J].
PLAGEMANN, PGW ;
MOENNIG, V .
ADVANCES IN VIRUS RESEARCH, 1992, 41 :99-192
[35]   A steady-state and pre-steady-state kinetic analysis of the NTPase activity associated with the hepatitis C virus NS3 helicase domain [J].
Preugschat, F ;
Averett, DR ;
Clarke, BE ;
Porter, DJT .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (40) :24449-24457
[36]   ATPASE AND GTPASE ACTIVITIES ASSOCIATED WITH SEMLIKI FOREST VIRUS NONSTRUCTURAL PROTEIN NSP2 [J].
RIKKONEN, M ;
PERANEN, J ;
KAARIAINEN, L .
JOURNAL OF VIROLOGY, 1994, 68 (09) :5804-5810
[37]  
Sambrook J., 2002, MOL CLONING LAB MANU
[38]   Biochemical characterization of the equine arteritis virus helicase suggests a close functional relationship between arterivirus and coronavirus helicases [J].
Seybert, A ;
van Dinten, LC ;
Snijder, EJ ;
Ziebuhr, J .
JOURNAL OF VIROLOGY, 2000, 74 (20) :9586-9593
[39]   The human coronavirus 229E superfamily 1 helicase has RNA and DNA duplex-unwinding activities with 5′-to-3′ polarity [J].
Seybert, A ;
Hegyi, A ;
Siddell, SG ;
Ziebuhr, J .
RNA, 2000, 6 (07) :1056-1068
[40]   Determination of the complete nucleotide sequence of a vaccine strain of porcine reproductive and respiratory syndrome virus and identification of the Nsp2 gene with a unique insertion [J].
Shen, S ;
Kwang, J ;
Liu, W ;
Liu, DX .
ARCHIVES OF VIROLOGY, 2000, 145 (05) :871-883