Nepoviruses: Molecular Biology and Replication

Mayo, M. A.; Robinson, D. J.

doi:10.1007/978-1-4899-1772-0_6

Cited by 52 publications

(41 citation statements)

References 160 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The duplication of proteins and the unusually large size (1545 nt in RNA1 and 1550 nt in RNA2) of the 3hNCRs are unique to TomRSV. Recently, TomRSV was placed in the nepovirus ' cluster c ' (Mayo & Robinson, 1996). The RNA2 sequences of known viruses in this subgroup (blueberry leaf mottle virus, cherry leafroll virus, TomRSV) have long ( 1300 nt) 3hNCRs, unlike SDV.…”

Section: Hjementioning

confidence: 99%

Nucleotide sequences and taxonomy of satsuma dwarf virus.

Iwanami

Kondo

Karasev

1999

Journal of General Virology

View full text Add to dashboard Cite

The nucleotide sequences of genomic RNA1 (6795 nt) and RNA2 (5345 nt) of satsuma dwarf virus (SDV), a tentative member of the genus Nepovirus, were determined. The deduced genome organization of SDV showed similarities to the organization in como-, faba-and nepoviruses. There is extensive amino acid sequence similarity in the N-terminal regions of the proteins encoded by RNA1 and RNA2, as reported previously only for tomato ringspot nepovirus. However, unlike definitive nepoviruses, which have a single coat protein, SDV has two coat proteins. SDV RNA2 does not contain the long ( 1300 nt) 3h non-coding region characteristic of some nepoviruses. Phylogenetic analysis of SDV RNA polymerase placed SDV apart from como-, faba-and nepoviruses. These unique features suggest that SDV is distinct from the Comovirus, Fabavirus and Nepovirus genera, and needs to be separated into a new genus, probably within the family Comoviridae.

show abstract

Section: Hjementioning

confidence: 99%

Nucleotide sequences and taxonomy of satsuma dwarf virus.

Iwanami

Kondo

Karasev

1999

Journal of General Virology

View full text Add to dashboard Cite

show abstract

“…Each RNA is covalently attached to a small virusencoded protein (VPg, viral genome-linked protein) at the 5h end. Nepoviruses have been subdivided into three subgroups (Mayo & Robinson, 1996) and TomRSV is the only member of nepovirus subgroup c for which the entire nucleotide sequence is known. RNA-1 contains a single long open reading frame beginning at an AUG codon at nucleotide position 78 (Rott et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

“…In particular, a histidine residue located in the Cterminal region of the protease is directly involved in the recognition of a glutamine (or glutamate) residue at the k1 position of the cleavage sites of picorna-, poty-and comovirus polyproteins (Bazan & Fletterick, 1988 ;Gorbalenya et al, 1989 ;Allaire et al, 1994 ;Matthews et al, 1994 ;Ivanoff et al, 1986 ;Dougherty et al, 1989 ;. The proteases of nepoviruses of subgroups a and b do not contain a histidine residue in their substrate-binding pockets and recognize cleavage sites that differ from the (Q, E)\(G, S, M) consensus of the aforesaid polyproteins (see Mayo & Robinson, 1996 ;Sanfaçon, 1995 and references therein). We previously reported that the cleavage site between the TomRSV movement protein and coat protein is Q\G and suggested that the cleavage sites of the TomRSV polyprotein more closely resemble the picorna-, como-and potyvirus cleavage sites than the cleavage sites of polyproteins from nepoviruses of subgroups a and b .…”

Section: Introductionmentioning

confidence: 99%

Proteolytic processing of tomato ringspot nepovirus 3C-like protease precursors: definition of the domains for the VPg, protease and putative RNA-dependent RNA polymerase.

Wang

Carrier

Chisholm³

et al. 1999

Journal of General Virology

View full text Add to dashboard Cite

“…Each RNA is covalently linked to a small virus-encoded protein (VPg) at its 5Ј end and encodes one large polyprotein. Nepoviruses have a genomic organization similar to that of the animal picornaviruses (34,44). The RNA1-encoded polyprotein (P1) contains the domains for proteins likely to be involved in replication, including a putative nucleoside triphosphate binding (NTB) protein, the VPg, the 3C-like proteinase (Pro), and the RNA-dependent RNA polymerase (Pol) (Fig.…”

mentioning

confidence: 99%

Tomato Ringspot Virus Proteins Containing the Nucleoside Triphosphate Binding Domain Are Transmembrane Proteins That Associate with the Endoplasmic Reticulum and Cofractionate with Replication Complexes

Han

Sanfaçon²

2003

J Virol

View full text Add to dashboard Cite

Replication of all known positive-strand RNA viruses occurs in replication complexes associated with intracellular membranes. The putative nucleoside triphosphate binding (NTB) protein of Tomato ringspot virus (ToRSV) contains a stretch of hydrophobic residues at its C terminus, suggesting that it may act as a membrane anchor for the replication complex. Anti-NTB antibodies detected two predominant proteins in membrane-enriched fractions (the 66-kDa NTB and 69-kDa NTB-VPg proteins) along with other, larger proteins. The proteins containing the NTB domain cofractionated with markers of the endoplasmic reticulum (ER) and with ToRSV-specific RNA-dependent RNA polymerase activity in sucrose gradients. ToRSV infection induced severe changes in the morphology of the ER in plants expressing an ER-targeted green fluorescent protein (ER-GFP), and proteins containing the NTB domain colocalized with ER-GFP in indirect immunofluorescence assays. The proteins containing the NTB domain have properties of integral membrane proteins. Proteinase K protection assays using purified membranes from infected plants revealed that although the central portion of the NTB domain is exposed to the cytoplasmic face of the membranes, an 8-kDa fragment, recognized by anti-VPg antibodies, is protected by the membranes. This fragment probably consists of the 3-kDa VPg and the 5-kDa stretch of hydrophobic residues at the C terminus of the NTB protein, suggesting a luminal location for the VPg in at least a portion of the molecules. These results provide evidence that proteins containing the NTB domain are transmembrane proteins associated with ER-derived membranes and support the hypothesis that one or several of the proteins containing the NTB domain anchor the replication complex to the ER.Replication of the genomes of all characterized positivestrand RNA viruses occurs in large complexes which are associated with intracellular membranes (5). Many positive-strand RNA viruses induce extensive proliferation and modification of intracellular membranes in their hosts, which often results in the accumulation of numerous membranous vesicles. Doublestranded RNA (dsRNA) replication intermediates and viral replication factors are associated with the membranous vesicles, which are thought to be the site of the replication (6,7,18,25,48,49,52). The requirement for intact membranes for successful virus replication has also been demonstrated using cell-free replication systems (2, 35, 59). Different viruses associate with and modify different types of intracellular membranes (5). Although the importance of the association of viral replication factors with intracellular membranes is well documented, the mechanisms by which replication complexes are fixed on specific membrane sites remain poorly understood.Picornaviruses and several plant viruses with similar genomic organization have been shown to replicate in association with membranes derived from the endoplasmic reticulum (ER) (6,42,47,51). One or several viral proteins are thought to act as membrane an...

show abstract

Nepoviruses: Molecular Biology and Replication

Cited by 52 publications

References 160 publications

Nucleotide sequences and taxonomy of satsuma dwarf virus.

Nucleotide sequences and taxonomy of satsuma dwarf virus.

Proteolytic processing of tomato ringspot nepovirus 3C-like protease precursors: definition of the domains for the VPg, protease and putative RNA-dependent RNA polymerase.

Tomato Ringspot Virus Proteins Containing the Nucleoside Triphosphate Binding Domain Are Transmembrane Proteins That Associate with the Endoplasmic Reticulum and Cofractionate with Replication Complexes

Contact Info

Product

Resources

About