Coat protein of Potyviruses

Shukla, D. D.; Thomas, J. E.; McKern, Neil M.; Tracy, Samantha Lilly; Ward, Colin W.

doi:10.1007/bf01310826

Cited by 43 publications

(7 citation statements)

References 33 publications

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“…This apparent discrepancy could be resolved if potato virus Y-D is transmissible at a very low level; alternatively, it could be that the context within which the glutamate residue occurs may alter the effect on aphid transmissibility. There are non-aphidtransmissible potyvirus isolates in which the Asp-Ala-Gly triplet is conserved (30,34). For potato virus Y-18, the residue after the glycine differs from that in transmissible isolates (30 , Table 3), whereas zucchini yellow mosaic virus-CT differs from an aphid-transmissible isolate in the residue preceding the aspartate of the triplet (34 , Table 3).…”

Section: Discussionmentioning

confidence: 99%

“…There are non-aphidtransmissible potyvirus isolates in which the Asp-Ala-Gly triplet is conserved (30,34). For potato virus Y-18, the residue after the glycine differs from that in transmissible isolates (30 , Table 3), whereas zucchini yellow mosaic virus-CT differs from an aphid-transmissible isolate in the residue preceding the aspartate of the triplet (34 , Table 3). Whether loss of aphid transmissibility is due to these or other mutations that affect amino acid residues in the N terminus of the coat protein or to mutations in the helper component gene (36), which codes for a protein essential for aphid transmission of potyviruses, remains to be determined.…”

Section: Discussionmentioning

confidence: 99%

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Amino acid substitutions in the coat protein result in loss of insect transmissibility of a plant virus.

Atreya

Pirone

1991

Proc. Natl. Acad. Sci. U.S.A.

219

117

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Amino acids near the N terminus of the coat protein of tobacco vein mottling virus were deleted or altered by site-directed mutagenesis to determine the effect on aphid transmissibility of the virus. Deletion of a three amino acid sequence Asp-Ala-Gly, which is conserved in aphidtransmissible potyvirus isolates, abolished transmission. The mutation Ala --Thr in this triplet drastically reduced transmission, whereas the mutation Asp --Asn had no effect, and the mutation Asp -' Lys consistently reverted to the wild-type residue. The mutation Lys--Glu, in the residue adjacent to the glycine ofthe triplet, drastically reduced transmission, whereas the mutation Gin -+ Pro, seven residues downstream from the glycine had no effect. Comparison of the sequences of other potyviruses suggests that the presence ofa glycine residue at the third position of the Asp-Ala-Gly triplet is critical for aphid transmissibility and that certain changes in the residues adjacent to this position abolish or greatly reduce aphid transmissibility.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Amino acid substitutions in the coat protein result in loss of insect transmissibility of a plant virus.

Atreya

Pirone

1991

Proc. Natl. Acad. Sci. U.S.A.

219

117

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“…It should be possible to identify the epitopes responsible for the unexpected and inconsistent "paired" relationships reported between independent potyviruses (2-5, 8, 13) and to establish the cause for the very poor serological cross-reactivity between pepper mottle virus and strains of PVY despite their very close sequence homology (3,6). In turn it should lead to the use of synthetic peptides corresponding to defined epitopes, to generate virus-specific and group-specific serological probes.…”

Section: Discussionmentioning

confidence: 99%

“…During investigations on the structural characterization of the coat proteins of potyviruses we made the following observations that have implications for potyvirus detection and classification: (i) distinct potyviruses exhibit coat protein sequence homology of 38-71% with major differences in the length (29-95 residues) and sequence of the N-terminal portion of their coat proteins but high sequence homology (65%) in the C-terminal three-quarters ofthe coat proteins (5); (ii) strains of individual viruses exhibit very high sequence homology (90-99%) (5)(6)(7)(8); (iii) the N and C termini of the coat proteins are surface-located as found for other rod-shaped plant viruses such as tobamoviruses, potexviruses, and tobraviruses and can be removed from virions by mild proteolysis (8,9).…”

mentioning

confidence: 99%

Localization of virus-specific and group-specific epitopes of plant potyviruses by systematic immunochemical analysis of overlapping peptide fragments.

Shukla

Tribbick²,

Mason³

et al. 1989

Proc. Natl. Acad. Sci. U.S.A.

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Virus-specific or group-specific antibody probes to potyviruses can be produced by targeting the immune response to the virus-specific, N-terminal region of the capsid protein (29-95 amino acids depending on the virus) or to the conserved core region (216 amino acids) of the capsid protein, respectively. Immunochemical analysis of overlapping, synthetic octapeptides covering the capsid protein of the Johnsongrass strain of Johnsongrass mosaic virus (JGMV-JG) has delineated the peptide sequences recognized by five polyclonal rabbit antisera and two mouse monoclonal antibodies (mAbs). The antibodies characterized were (i) three virus-specific rabbit polyclonal antisera and one virus-specific mouse mAb (1/25) raised against native virus particles, (ii) one polyclonal antiserum raised against trypsin-derived core particles of JGMV-JG, (iii) one group-specific polyclonal antiserum raised against the denatured, truncated coat protein from trypsinderived core particles of JGMV-JG, and (iv) one group-specific mouse mAb (1/16) raised against native virus particles. The two epitopes seen by mAb 1/25 occurred at residues 18-27 and 43-52 and overlapped with the two major epitopes seen by the virus-specific polyclonal antiserum. The group-specifilc epitope seen in JGMV-JG by mAb 1/16 was also recognized strongly in potato virus Y. the type member of the potyvirus group. The multiple epitopes seen by the cross-reactive polyclonal antisera were distributed across the entire core region of the coat protein and their relative antibody binding responses varied between JGMV-JG, potato virus Y, and six other distinct potyviruses.Plant diseases are estimated to be responsible for economic losses worldwide of $60 billion per annum (1). The most important pathogens are fungi, with plant viruses the second most important group of infectious agents. Of the 28 plant virus groups or families the potyvirus group is the largest. It contains at least 175 independent members and accounts for about 30% of all viruses known to infect plant species around the world (2, 3). Potyvirus particles are flexuous rods, 729-900 nm long and -11 nm in diameter, and consist of up to 2000 subunits of a single protein species (4).Successful control and eradication of plant virus infections is dependent on the availability of simple, reliable methods for plant virus detection and identification. To date, this has been difficult to achieve for potyviruses due to the large size of the group, the vast variation between members, and the lack of satisfactory taxonomic parameters to distinguish independent viruses from related strains (2-4). Thus, there is a real need to evaluate new criteria for the identification and classification of potyviruses.During investigations on the structural characterization of the coat proteins of potyviruses we made the following observations that have implications for potyvirus detection and classification: (i) distinct potyviruses exhibit coat protein sequence homology of 38-71% with major differences in the length (29-95 re...

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“…The CP structure comprises three domains (Baratova et al, 2001;Shukla et al, 1988). The central domain called the core CP interacts with viral RNA in matured virions.…”

Section: Capsid Proteinmentioning

confidence: 99%

Unfolding the secrets of plum pox virus: from epidemiology to genomics

Šubr¹,

Glasa²

2013

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Summary. -Over an approximately 80-year period since the description of the Sharka disease, the plum pox virus (PPV) has been thoroughly studied on various levels of the infection cycle. World-wide distribution of the virus, severity of the disease for the fruit industry with a potential to be further increased and discovery/ emergence of new strains make PPV the most epidemiologically important viral pathogen of stone fruit trees. The history of PPV research reflects the development of analytical methods applicable in plant virology. In particular the establishment of molecular biology with reverse genetics and improvement of DNA sequencing technology have further contributed to the increase in knowledge on PPV variability, evolution, replication and interaction with host plants. This review gives a comprehensive summary of PPV data accumulated progressively, from the biological characterization of the disease to recent attempts aimed at using the PPV-based vectors for expression of exogenous proteins in plants.

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Coat protein of Potyviruses

Cited by 43 publications

References 33 publications

Amino acid substitutions in the coat protein result in loss of insect transmissibility of a plant virus.

Amino acid substitutions in the coat protein result in loss of insect transmissibility of a plant virus.

Localization of virus-specific and group-specific epitopes of plant potyviruses by systematic immunochemical analysis of overlapping peptide fragments.

Unfolding the secrets of plum pox virus: from epidemiology to genomics

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