The nucleotide sequence of tomato ringspot nepovirus (TomRSV) RNA1 has been determined. TomRSV RNA1 is 8214 nucleotides in length, excluding the 3′ poly(A) tail, and contains a single long open reading frame (ORF) of 6591 nucleotides beginning at the first AUG codon at nucleotide position 78. This ORF accounts for 80% of the RNA1 sequence and would give rise to a polyprotein with a predicted molecular mass of 244 kDa. Amino acid sequence comparisons between portions of the TomRSV RNA1-encoded polyprotein and proteins encoded by several members of the picornavirus superfamily have provided information concerning the genomic organization and putative functions of TomRSV-encoded proteins. The putative TomRSV protease retains a conserved histidine residue present in the proteases encoded by members of the como-, poty- and poliovirus groups which is thought to be involved in dipeptide cleavage site recognition. Interestingly, this histidine residue is replaced by a leucine in the proteases of other sequenced nepoviruses. This suggests that the TomRSV protease shares dipeptide cleavage site specificity with that of como-, poty- and picornaviruses rather than the other nepoviruses.
AllisonR.,
JohnstonD. E.,
DoughertyW. G.1986; The nucleotide sequence of the coding region of tobacco etch virus genomic RNA: evidence for the synthesis of a single polyprotein. Virology 154:9–20
ArgosP.,
KamerG.,
NiklinM. J. H.,
WimmerE.1984; Similarity in gene organization and homology between proteins of animal picornaviruses and a plant comovirus suggest common ancestry of these virus families. Nucleic Acids Research 12:7251–7267
BazanJ. F.,
FletterickR. J.1988; Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications. Proceedings of the National Academy of Sciences, USA 85:7872–7876
DemangeatG.,
GrieffC.,
HemmerO.,
FritschC.1990; Analysis of the in vitro cleavage products of the tomato black ring virus RNA-l-encoded 250K polyprotein. Journal of General Virology 71:1649–1654
DorssersL.,
Van der KrolS.,
van der MeerJ.,
van KammenA.,
ZabelP.1984; Purification of cowpea mosaic virus RNA replication complex: identification of a virus-encoded 110, 000 dalton polypeptide responsible for RNA chain elongation. Proceedings of the National Academy of Sciences, USA 81:1951–1955
GoldbachR.,
RezelmanG.1983; Orientation of the cleavage maps of the 200-kilodalton polypeptide encoded by the bottom component RNA of cowpea mosaic virus. Journal of Virology 46:614–619
GoldbachR.,
van KammenA.1985; Structure, replication and expression of the bipartite genome of cowpea mosaic virus. In Molecular Plant Virology vol 2 pp 83–120 Edited by
DaviesJ. W.
Boca Raton, FL: CRC Press;
GorbalenyaA. E.,
BlinovV. M.,
DonchenkoA. P.,
KooninE. V.1989a; An NTP-binding motif is the most conserved sequence in a highly diverged monophyletic group of proteins involved in positive strand RNA viral replication. Journal of Molecular Evolution 24:256–268
HammerleT.,
HellenC. U. T.,
WimmerE.1991; Site-directed mutagenesis of the putative catalytic triad of poliovirus 3C proteinase. Journal of Biological Chemistry 266:5412–5416
MargisR.,
PinckL.1992; Effects of site-directed mutagenesis on the presumed catalytic triad and substrate-binding pocket of grapevine fanleaf nepovirus 24-kDa proteinase. Virology 190:884–888
MargisR.,
ViryM.,
PinckM.,
BardonnetN.,
PinckL.1994; Differential proteolytic activities of precursor and mature forms of the 24K proteinase of grapevine fanleaf nepovirus. Virology 200:79–86
MartelliG. P.1975; Some features of nematode-borne viruses and their relationship with the host plants. In Nematode-borne Vectors of Plant Viruses pp 223–252 Edited by
LambertiF.,
TaylorC. E.,
SeinhortJ. W.
London & New York: Plenum Press;
PetersS. A.,
VoorhorstW. G. B.,
WeryJ.,
WellinkJ.,
van KammenA.1992; A regulatory role for the 32K protein in proteolytic processing of cowpea mosaic virus polyproteins. Virology 191:81–89
PinckM.,
ReinboltJ. A. M.,
LoudesA. M.,
Le RetM.,
PinckL.1991; Primary structure and location of the genome-linked protein (VPg) of grapevine fanleaf nepovirus. FEBS Letters 284:117–119
RacanielloV. R.,
BaltimoreD.1981; Molecular cloning of poliovirus cDNA and determination of the complete nucleotide sequence of the viral genome. Proceedings of the National Academy of Sciences, USA 78:4887–4891
RottM. E.,
TremaineJ. H.,
RochonD. M.1991b; Comparison of the 5′ and 3′ termini of tomato ringspot virus RNA1 and RNA2: evidence for RNA recombination. Virology 185:468–472
ScottN. W.,
CooperJ. I.,
LiuY. Y.,
HellenC. U. T.1992; A 1.5 kb sequence homology in the 3′-terminal regions of RNA-1 and RNA-2 of a birch isolate of cherry leaf roll nepovirus is also present, in part, in a rhubarb isolate. Journal of General Virology 73:481–485
TakedaN.,
KuhnR. J.,
YangC. F.,
TakegamiT.,
WimmerE.1986; Initiation of poliovirus plus-strand RNA synthesis in a membrane complex of infected HeLa cells. Journal of Virology 60:43–53
VosP.,
VerverJ.,
JaegleM.,
WellinkP.,
GoldbachR.1988; Two viral proteins involved in the proteolytic processing of the cowpea mosaic virus polyprotein. Nucleic Acids Research 16:1967–1985
WellinkJ.,
RezelmanG.,
GoldbachR.,
BeyreutherK.1986; Determination of the proteolytic processing sites in the polyprotein encoded by the bottom-component of cowpea mosaic virus. Journal of Virology 59:50–58
WieczorekA.,
SanfaconH.1993; Characterization and subcellular localization of tomato ringspot nepovirus putative movement protein. Virology 194:734–742
ZabelP.,
MoermanM.,
LomonossoffG.,
ShanksM.,
BeyreutherK.1984; Cowpea mosaic virus VPg: sequencing of radiochemically modified protein allows mapping of the gene on B RNA. EMBO Journal 3:1629–1634