Andean Potato Mottle, a New Member of the Cowpea Mosaic Virus Group

Fribourg, C. E.; Jones, R. A. C.; Koenig, R.

doi:10.1094/phyto-67-969

Cited by 36 publications

(23 citation statements)

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“…Andean potato mottle virus (APMoV) is a plant virus endemic in South America (1) and a member of the Comovirus genus and Comoviridae family, of which cowpea mosaic virus (CPMV) is the type member (2). APMoV infects economically important Solanaceae plants, such as potato, tomato, eggplant and pepper.…”

Section: Introductionmentioning

confidence: 99%

“…APMoV infects economically important Solanaceae plants, such as potato, tomato, eggplant and pepper. The symptoms produced by APMoV infection include mild to severe mottling, systemic necrotic spots, leaf deformation, and plant stunting (1). The genomic structure of APMoV consists of two plus-stranded RNA molecules, designated as RNA-1 and RNA-2, of 5.6 kb (3) and 3.5 kb (4), respectively.…”

Section: Introductionmentioning

confidence: 99%

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The 42-kDa coat protein of Andean potato mottle virus acts as a transcriptional activator in yeast

Margis

2002

Braz J Med Biol Res

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Interactions of viral proteins play an important role in the virus life cycle, especially in capsid assembly. Andean potato mottle comovirus (APMoV) is a plant RNA virus with a virion formed by two coat proteins (CP42 and CP22). Both APMoV coat protein open reading frames were cloned into pGBT9 and pGAD10, two-hybrid system vectors. HF7c yeast cells transformed with the p9CP42 construct grew on yeast dropout selection media lacking tryptophan and histidine. Clones also exhibited ß-galactosidase activity in both qualitative and quantitative assays. These results suggest that CP42 protein contains an amino acid motif able to activate transcription of His3 and lacZ reporter genes in Saccharomyces cerevisiae. Several deletions of the CP42 gene were cloned into the pGBT9 vector to locate the region involved in this activation. CP42 constructions lacking 12 residues from the C-terminal region and another one with 267 residues deleted from the N-terminus are still able to activate transcription of reporter genes. However, transcription activation was not observed with construction p9CP42DC57, which does not contain the last 57 amino acid residues. These results demonstrate that a transcription activation domain is present at the C-terminus of CP42 between residues 267 and 374.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

The 42-kDa coat protein of Andean potato mottle virus acts as a transcriptional activator in yeast

Margis

2002

Braz J Med Biol Res

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“…Its iso metric RNA-containing particles measure about 28 nm in diameter, and are composed to similar amounts, on a molar basis, of two poly peptides with molecular weights of 22 kD (small coat protein, SCP) and 42 kD (large coat protein, LCP) [1,2].…”

Section: Introductionmentioning

confidence: 99%

Nucleotide Sequence Analysis of an Andean Potato Mottle Virus Middle Component RNA cDNA Clone: Comparisons of the Encoded Proteins with Those of Other Comoviruses

et al. 1993

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Andean potato mottle virus (APMV) is a comovirus whose genomic structure consists of two plus-strand RNA molecules (M- and B-RNA). Here we report the nucleotide sequence analysis of an APMV M-RNA cDNA clone with 3,669 nucleotide (nt) residues, exclusive of the polyadenylate at the 3’ end, covering approximately 99% of the APMV M-RNA. The first initiation codon in register translates from nt 194 to 3185 a polyprotein of 997 amino acid (aa) residues. A second initiation codon in register, beginning at nt position 416, translates a polyprotein of 923 aa. The cleavage sites used in the processing of polyprotein were identified in the long open reading frame by N-terminal microsequencing of the large coat protein (LCP) and the small coat protein (SCP). These dipeptide cleavage sites are Q/M for the LCP and Q/F for the SCP. In a comparison of the deduced APMV polyprotein aa sequence with those of four other comoviruses, the coding regions for the putative movement protein, LCP and SCP, were found similar in length in all five species. Multiple alignment of the M-RNA sequences for each of the three genes from the five comoviruses revealed different degrees of homology. APMV was always the least homologous of the five comoviruses, showing significant aa substitutions in positions where the other comoviruses have identical residue or conservative substitutions.

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“…This virus was first described in Peru by Fribourg et al (1977). APMV has a bipartite genome, consisting of two plus-strand RNA molecules denominated M RNA (3.5 kb) and B RNA (5.6 kb).…”

mentioning

confidence: 99%

“…APMV has a bipartite genome, consisting of two plus-strand RNA molecules denominated M RNA (3.5 kb) and B RNA (5.6 kb). Both genomic RNAs are separately encapsidated into icosahedral particles, built up by two coat proteins (Fribourg et al, 1977). The comovirus genome is translated into a large polyprotein from which the mature proteins are released upon cleavage by a virusencoded protease (Franssen et al, 1984;Goldbach et al, 1981).…”

mentioning

confidence: 99%

Molecular cloning and sequence analysis of a segment from Andean potato mottle virus B RNA encoding the putative RNA polymerase

Krengiel

Vincente²,

Weyne³

et al. 1993

Journal of General Virology

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Andean Potato Mottle, a New Member of the Cowpea Mosaic Virus Group

Cited by 36 publications

References 0 publications

The 42-kDa coat protein of Andean potato mottle virus acts as a transcriptional activator in yeast

The 42-kDa coat protein of Andean potato mottle virus acts as a transcriptional activator in yeast

Nucleotide Sequence Analysis of an Andean Potato Mottle Virus Middle Component RNA cDNA Clone: Comparisons of the Encoded Proteins with Those of Other Comoviruses

Molecular cloning and sequence analysis of a segment from Andean potato mottle virus B RNA encoding the putative RNA polymerase

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