Nucleotide sequence at the 3′ terminus of pepper mottle virus genomic RNA: Evidence for an alternative mode of potyvirus capsid protein gene organization

Dougherty, William G.; Allison, Richard F.; Parks, T. Dawn; Johnston, Robert E.; Feild, Mark J.; Armstrong, F. B.

doi:10.1016/0042-6822(85)90011-x

Cited by 81 publications

(47 citation statements)

References 27 publications

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“…The CP of the PPV-NAT isolate has a deletion of 15 amino acids near the N terminus. All PPV CPs are larger than those of other potyviruses like sugarcane mosaic virus (SCMV; Gough et al, 1987), pepper mottle virus (PeMV; Dougherty et al, 1985), TVMV (Domier et al, 1986), TEV (Allison et al, 1986) and potato virus Y (Shukla et al, 1986). The larger CP is reflected in the extended nucleotide sequence of PPV-NAT compared to TVMV and TEV.…”

Section: Qpppviqpaprttapmlnpiftpattqpatkpvsqvsgpqmentioning

confidence: 95%

“…10 kb (Hollings & Brunt, 1981). Several investigations have demonstrated that post-translational proteolytic processing of polyproteins is the mechanism of potyviral genome expression (Dougherty et al, 1985;Allison et aL, 1986;Carrington & Dougherty, 1987;Hellmann et al, 1988 ;Chang et al, 1988). The positions of functional virus proteins in the polyprotein have been proposed for tobacco vein mottling virus (TVMV) (Domier et al, 1986), helper component protein (HC), cylindrical inclusion protein (CI), two nuclear inclusion proteins (NIa and NI0 and the coat protein (CP).…”

Section: Introductionmentioning

confidence: 99%

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The Complete Nucleotide Sequence of Plum Pox Virus RNA

Maiß¹,

Timpe²,

Brisske³

et al. 1989

Journal of General Virology

209

143

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SUMMARYThe complete nucleotide sequence of the RNA of an aphid non-transmissible plum pox virus (PPV-NAT) isolate has been determined from five overlapping cDNA clones, cDNA prepared by primer extension was used to determine the 5' terminus. The assembled RNA is 9741 nucleotides in length, excluding a 3' terminal poly(A) sequence. One large open reading frame starts at nucleotide positions 36 to 38 and is terminated with an UAG codon at positions 9522 to 9524. The putative start codon is located at positions 147 to 149. The encoded polyprotein has a predicted Mr of 353"8K. Comparison of cistrons from tobacco vein mottling virus and tobacco etch virus with those predicted for PPV-NAT indicated a similar genome organization. A highly conserved sequence of 12 nucleotides was found in the 5' non-coding region of these three potyviruses. The potential polyadenylation signal from yeast (UAUGU) was found in the 3' non-coding region of PPV-NAT and several other members of the potyvirus group.

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Section: Qpppviqpaprttapmlnpiftpattqpatkpvsqvsgpqmentioning

confidence: 95%

Section: Introductionmentioning

confidence: 99%

The Complete Nucleotide Sequence of Plum Pox Virus RNA

Maiß¹,

Timpe²,

Brisske³

et al. 1989

Journal of General Virology

209

143

View full text Add to dashboard Cite

show abstract

“…Our results demonstrate that such enzyme treatment readily removed both N-and C-terminal regions of the coat proteins and hence that both these regions are exposed on the surface of potyvirus particles. Dougherty and co-workers (Allison et aL, 1985a;Dougherty et aL, 1986b) were the first to show that mild trypsin treatment of potyvirus particles removed exposed surface epitopes. They found that such enzymic digestion removed 29 amino acid residues from the N terminus of TEV coat protein and abolished the binding site for anti-TEV monoclonal antibodies.…”

Section: Discussionmentioning

confidence: 99%

The N and C Termini of the Coat Proteins of Potyviruses Are Surface-located and the N Terminus Contains the Major Virus-specific Epitopes

Shukla

Strike

Tracy

et al. 1988

Journal of General Virology

281

241

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SUMMARYMild proteolysis by trypsin of particles of six potyviruses (bean yellow mosaic virus, clover yellow vein virus, Johnson grass mosaic virus, passion-fruit woodiness virus, potato virus Y and watermelon mosaic virus II) revealed that the N-and C-terminal regions of their coat protein are exposed on the particles' surfaces. The enzyme treatment removed the N-terminal region (30 to 67 amino acids long, depending on the virus) and 18 to 20 amino acids from the C terminus of the coat proteins, leaving a fully assembled virus particle composed of coat protein cores consisting of 216 or 218 amino acid residues. These core particles were indistinguishable from untreated native particles in an electron microscope and were still infectious. The core particles lacked the virus-specific surface epitopes that are recognized by the bulk of the polyclonal antibodies raised against the whole virus particles. Epitopes thought to be groupspecific were located in the trypsin-resistant core protein region. The implications of these findings are discussed in relation to the similar surface location of the N-and Cterminal regions of the coat protein of other rod-shaped plant viruses and the observed common structural features displayed by isometric plant and animal viruses.

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“…The deduced amino acid sequence of the TuMV capsid protein was compared, among others, with those previously determined for the capsid protein of sugarcane mosaic virus (ScMV) (Gough et al, 1987), pepper mottle virus (PeMV) (Dougherty et al, 1985), PVY (van der Vlugt et al, 1989), TVMV (Domier et al, 1986) and PPV (Lain et al, 1988;Maiss et al, 1988). Alignment of these sequences revealed the presence of very highly conserved regions.…”

mentioning

confidence: 99%