Evidence that a component other than the virus particle is needed for aphid transmission of potato virus Y

Govier, D. A.; Kassanis, B.

doi:10.1016/0042-6822(74)90129-9

Cited by 71 publications

(23 citation statements)

References 3 publications

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“…Several species of aphid vectors (especially Aphis, Myzus, and Macrosiphum species) are often implicated in the widespread occurrence of potyviruses in a number of crops; this is probably attributable to their fecundity, polyphagy, and mobility in immature crops [51]. Although little is known about the molecular mechanisms of aphid transmissibility, transmission is known to be dependent on the presence within infected plants of a virus-coded helper component protein of M r 53-58k [25,56,57,68] and also, with some viruses at least, the composition of the capsid protein [3,55].…”

Section: Natural Transmissionmentioning

confidence: 99%

The general properties of potyviruses

Brunt

1992

Potyvirus Taxonomy

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Section: Natural Transmissionmentioning

confidence: 99%

The general properties of potyviruses

Brunt

1992

Potyvirus Taxonomy

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“…HC-Pro is a suppressor of RNA silencing and considered to be an important determinant of virus-host interactions (Anandalakshmi et al, 1998;Brigneti et al, 1998;Kasschau & Carrington, 1998;Torres-Barceló et al, 2008;reviewed by Rajamäki et al, 2004). HC-Pro is also necessary for transmission of potyviruses by aphids (Govier & Kassanis, 1974;Blanc et al, 1998;Wang et al, 1998). The lack of HC-Pro in three ipomoviruses raises questions about the importance of this protein for SPMMV.…”

Section: Introductionmentioning

confidence: 99%

Recombination and selection pressure in the ipomovirus sweet potato mild mottle virus (Potyviridae) in wild species and cultivated sweetpotato in the centre of evolution in East Africa

Tugume

Mukasa

Kalkkinen

et al. 2009

Journal of General Virology

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Sweet potato mild mottle virus (SPMMV) is the type member of the genus Ipomovirus (family Potyviridae). SPMMV occurs in cultivated sweetpotatoes (Ipomoea batatas Lam.; Convolvulaceae) in East Africa, but its natural wild hosts are unknown. In this study, SPMMV was detected in 283 (9.8 %) of the 2864 wild plants (family Convolvulaceae) sampled from different agro-ecological zones of Uganda. The infected plants belonged to 21 species that were previously not known to be natural hosts of SPMMV. The size of the SPMMV coat protein (CP) was determined by Western blot analysis, N-terminal protein sequencing and peptide mass fingerprinting. Data implicated a proteolytic cleavage site, VYVEPH/A, at the NIb/CP junction, resulting in a CP of approximately 35 kDa. Nearly complete sequences of 13 SPMMV isolates were characterized. Phylogenetic analysis of non-recombinant CP-encoding sequences placed five isolates from wild species sampled in the central zone of Uganda into a separate cluster. Recombination events were detected in the 59-and 39-proximal parts of the genome, providing novel evidence of recombination in the genus Ipomovirus. Thirteen amino acids in the N terminus of the P1 protein were under positive selection, whereas purifying selection was implicated for the HC-Pro-, P3-, 6K1-and CP-encoding regions. These data, supported by previous studies on ipomoviruses, provide indications of an evolutionary process in which the P1 proteinase responds to the needs of adaptation.

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“…13) and presents many similarities with that of caulimoviruses. A nonstructural virus-encoded molecule, designated the "helper component" (HC), facilitates in part potyvirus aphid transmission (14,15). Characterized HCs have molecular masses ranging from 52 to 58 kDa and their active form is believed to be a soluble homodimer (16).…”

mentioning

confidence: 99%

Interaction between the aphid transmission factor and virus particles is a part of the molecular mechanism of cauliflower mosaic virus aphid transmission.

Schmidt

Blanc

Espérandieu

et al. 1994

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

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Cauliflower mosaic virus (CaMV) aphid transmission factor (ATF or P18) is presumed to interact with both virus particles and vector mouthparts, thereby mediating virus aphid transmission. We developed a protein-protein binding assay and our results clearly show that virus particles bind strongly and specifically to P18 whether P18 was obtained from plants, a baculovirus expression system, or the pGEX-3X Escherichia coil expression system. We overproduced, using the pGEX-3X expression system, various fragments of P18 and thereby demonstrated that the C-terminal 31 amino acid residues are responsible for the interaction. Using PCR-based mutagenesis, 2 amino acid residues essential for interaction were identified. Point substitutions (amino adds 157 from Ile to Asn or 159 from Gly to Ser) were sufficient to abolish the interaction, whereas another mutation (amino acid 158 from He to Ser) had no effect on P18 virus binding. We evaluated whether there was a correlation between the ability of P18 to interact with CaMV particles and its biological activity. Aphid transmission assays were carried out and we demonstrated that the loss of the virus binding capacity had a dramatic effect on the ability of P18 to mediate aphid transmission. Thus, our results suggest that binding between P18 and virus particles is likely to be one ofthe molecular mechanisms involved in CaMV aphid transmission.

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Evidence that a component other than the virus particle is needed for aphid transmission of potato virus Y

Cited by 71 publications

References 3 publications

The general properties of potyviruses

The general properties of potyviruses

Recombination and selection pressure in the ipomovirus sweet potato mild mottle virus (Potyviridae) in wild species and cultivated sweetpotato in the centre of evolution in East Africa

Interaction between the aphid transmission factor and virus particles is a part of the molecular mechanism of cauliflower mosaic virus aphid transmission.

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