A point mutation in the coat protein abolishes aphid transmissibility of a potyvirus

Atreya, Chintamani D.; Raccah, B.; Pirone, T. P.

doi:10.1016/0042-6822(90)90389-9

Cited by 269 publications

(146 citation statements)

References 21 publications

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“…In the CP, a DAG amino acid motif at the N terminus is required for aphid-transmissibility (Atreya et al, 1990(Atreya et al, , 1991(Atreya et al, , 1995. Both termini of CP are exposed on the virion surface and affect long-distance movement (Dolja et al, 1994(Dolja et al, , 1995Lo!…”

Section: Introductionmentioning

confidence: 99%

Potyvirus helper component-proteinase and coat protein (CP) have coordinated functions in virus-host interactions and the same CP motif affects virus transmission and accumulation.

Andrejeva

Puurand

Merits

et al. 1999

Journal of General Virology

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Section: Introductionmentioning

confidence: 99%

Potyvirus helper component-proteinase and coat protein (CP) have coordinated functions in virus-host interactions and the same CP motif affects virus transmission and accumulation.

Andrejeva

Puurand

Merits

et al. 1999

Journal of General Virology

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“…The origin and properties of TVMV-AT and TVMV-NAT (DAE mutant) have been described (Atreya et al, 1990). The TEV-HAT isolate was that used in previous studies (Pirone, 1981 ;Pirone & Thornbury, 1983).…”

Section: Methodsmentioning

confidence: 99%

“…The non-transmissibility of the TVMV mutant, TVMV-NAT, resulted from a change in the highly conserved DAG sequence near the coat protein N terminus to DAE (Atreya et al, 1990), while the loss of HC activity in the PVY variant, PVC, was attributed to a lysine to glutamic acid mutation in the highly conserved KITC sequence in the HC-Pro region (Atreya et al,, 1992 a). The reason for lack of virion transmissibility and HC activity has not been determined, however.…”

Section: Introductionmentioning

confidence: 99%

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Loss of potyvirus transmissibility and helper-component activity correlate with non-retention of virions in aphid stylets

Wang

Ammar

Thornbury

et al. 1996

Journal of General Virology

100

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The hypothesis that loss of aphid transmissibility of potyvirus mutants is due to non-retention of virions in the mouthparts was tested by feeding aphids through membranes on purified virions of aphid transmissible (AT or HAT) and non-aphid- (HC). TVMV virions were detected, by electron microscopic examination of immunogoldlabelled thin sections, in the food canal or cibarium of 57 % of 28 aphids fed on the transmissible combination of TVMV-AT and functional HC, while no virions were found in these structures in 25 aphids fed on the nontransmissible combinations: TVMV-NAT and PVY HC, or TVMV-AT and PVC HC. Autoradiography of intact stylets allowed the examination of much larger numbers of aphids, fed on 125I-labelled TEV; 48 % of 523 aphids fed on the TEV-HAT and PVY HC combination retained label in the stylets; this correlated well with the percentage transmission in bioassays. In contrast, in non-transmissible combinations, label was found in the stylets of 0.77% of 389 aphids fed on TEV-NAT and PVY HC, and 1-35 % of 223 aphids fed on TEV-HAT and PVC HC. No differences were found in the overall amount of label in the bodies of aphids fed on the transmissible and non-transmissible combinations. There was a strong tendency for virions to be retained in the distal third of the stylets; 56 % of aphids positive for TVMV, and 82 % of those positive for TEV, had label in this area. These data support the concept that virions retained within the stylets are those that are primarily involved in potyvirus transmission.

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“…The ORF has an UGA stop codon at nt positions 9368-9370. All typical PVY consensus amino acid sequences are present, including an EVHHQ/A NIb/CP cleavage site, the aphidtransmission-related DAG triplet in the N-terminus of the CP region (aa 6-8 of the CP) [1] and the aphid-transmission-related KITC and PTK motifs in the helper component protein (HC-Pro) region (aa 49-52 and aa 307-309 of the HC-Pro) [3].…”

mentioning

confidence: 99%

Complete nucleotide sequence of a potato isolate of strain group C of Potato virus Y from 1938

Dullemans¹,

Cuperus²,

Verbeek³

et al. 2010

Arch Virol

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The complete genomic sequence of an isolate (PRI-509) of the C strain of Potato virus Y (PVY C ), which was originally isolated from potato in 1938, was elucidated. The genomic RNA of PRI-509 consists of 9699 nucleotides, with the capacity to encode a polyprotein of 3061 amino acids with a molecular mass of 337 kDa. This is the first full-length sequence of a PVY C isolate from potato that belongs to the C1 phylogenetic subgroup, which was previously thought to exclusively contain nonpotato isolates.Potato virus Y (PVY), the type member of the genus Potyvirus, was described for the first time in the early 1930s as the causal agent of a serious disease in potato [26]. PVY is one of the most common viruses of potato (Solanum tuberosum L.) and causes significant economic losses worldwide, especially in the production of seed potatoes. [12,16,24,25].PVY O and PVY C can be distinguished in potato cultivars bearing the resistance genes Ny tbr and Nc [7,25]. PVY C isolates are defined by the typical hypersensitive response they induce in potato cultivars carrying the Nc gene. PVY C causes systemic mosaic or stipple streak symptoms in potato [8] and is generally not considered a serious problem, since many potato cultivars appear to display a hypersensitive response (field resistance) to this strain [6]. A survey in France in 1985 showed an infection rate of less than 5% with PVY C , while for PVY O and PVY N , infection levels of 80 and 12%, respectively, were reported [13]. In the Netherlands, field surveys conducted from 1994 to 2007 showed similar results [28].PVY also causes diseases and production loss in pepper (Capsicum annuum L.) [22], tomato (Solanum lycopersicum L.) and tobacco crops [25]. For some isolates from pepper, a high level of sequence identity to PVY C from potato was found [11,15,22]. Based on biological data, RFLP restrictotypes and coat protein sequence data, these non-potato isolates were proposed to form a genetic cluster separate from the potato isolates [22].The plant virus collection at Plant Research International (PRI) was established in the early 1950s and includes several historical isolates assigned to different PVY strains. The PVY C isolate described in this study (PRI-509) was isolated from the Dutch potato variety 'Zeeuwse Blauwe' in the Netherlands in 1938 [10,23] and was maintained only in potato. It causes a very distinctive pattern of systemic necrotic lines and lesions, known as stipple streak,The nucleotide sequence reported in this article is available under GenBank accession number: EU563512.Electronic supplementary material The online version of this article

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A point mutation in the coat protein abolishes aphid transmissibility of a potyvirus

Cited by 269 publications

References 21 publications

Potyvirus helper component-proteinase and coat protein (CP) have coordinated functions in virus-host interactions and the same CP motif affects virus transmission and accumulation.

Potyvirus helper component-proteinase and coat protein (CP) have coordinated functions in virus-host interactions and the same CP motif affects virus transmission and accumulation.

Loss of potyvirus transmissibility and helper-component activity correlate with non-retention of virions in aphid stylets

Complete nucleotide sequence of a potato isolate of strain group C of Potato virus Y from 1938

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