Complex Formation between Potyvirus VPg and Translation Eukaryotic Initiation Factor 4E Correlates with Virus Infectivity

Léonard, Simon; Plante, Daniel; Wittmann, Sylvie; Daigneault, Nicole; Fortin, Marc; Laliberté, Jean‐François

doi:10.1128/jvi.74.17.7730-7737.2000

Cited by 277 publications

(234 citation statements)

References 71 publications

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“…The T⌬S van't Hoff component contributes nearly one-third to the overall value of ⌬G 0 (at 25°C), suggesting lesser dependence on electrostatic contributions and a greater conformational contribution in the PAP-VPg binding with hydrophobic residues less solvent-exposed in the combined structure. The fact that PAP-VPg interactions are enthalpically driven and entropically favored at biological temperatures supports previous observations by Baldwin et al (23) that, because PAP is a plant defense protein, it should be able to perform under unpredictable temperature conditions, given its accepted function as a ribosome depurinating agent (23 (26). Moreover, the binding domain on VPg was mapped to a stretch of 35 amino acids, and substitution of aspartic acid residue found within this region completely abolished interactions of VPg with eIF4E/iso4E (26).…”

Section: Discussionsupporting

confidence: 69%

“…The fact that PAP-VPg interactions are enthalpically driven and entropically favored at biological temperatures supports previous observations by Baldwin et al (23) that, because PAP is a plant defense protein, it should be able to perform under unpredictable temperature conditions, given its accepted function as a ribosome depurinating agent (23 (26). Moreover, the binding domain on VPg was mapped to a stretch of 35 amino acids, and substitution of aspartic acid residue found within this region completely abolished interactions of VPg with eIF4E/iso4E (26). Plants infected with a TuMV infectious cDNA (p35Tunos) showed viral symptoms with p35Tunos, whereas plants infected with p35TuD77N, a mutant that contained the aspartic acid substitution in the VPg domain that abolished the interaction with eIF4E/iso4E, remained symptomless, suggesting that VPg-eIF4E/iso4E interaction is a critical element for virus production (26).…”

Section: Discussionsupporting

confidence: 69%

“…VPg plays a pivotal role in the viral infection cycle, replication, and cell-to-cell movement and also has been implicated in overcoming viral resistance in plants (25). Interactions between VPg of TuMV and the eIFiso4E/ iso4F of Arabidopsis thaliana (26,27) suggest that VPg is important in the initiation of protein synthesis (28). Interactions between VPg and plant eIFiso4E and effects of eIFiso4G on these interactions have been characterized (29 -31).…”

Section: Pokeweed Antiviral Protein (Pap)mentioning

confidence: 99%

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Inhibition of Pokeweed Antiviral Protein (PAP) by Turnip Mosaic Virus Genome-linked Protein (VPg)

Domashevskiy

Mizumoto

Goss

2012

Journal of Biological Chemistry

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Pokeweed antiviral protein (PAP) from Phytolacca americana is a ribosome inactivating protein (RIP) and an RNA N‐glycosidase that removes specific purine residues from the sarcin/ricin (S/R) loop of large rRNA, arresting protein synthesis at the translocation step. PAP is also a cap‐binding protein, and is a potent antiviral agent against many plant, animal, and human viruses. To elucidate the mechanism of RNA depurination, and to understand how PAP recognizes and targets various RNAs, the interactions between PAP and Turnip mosaic virus genome linked protein (VPg) were investigated. VPg can function as a cap analog in cap‐independent translation, and potentially target PAP to uncapped IRES‐containing RNA. In this work, fluorescence spectroscopy and HPLC techniques were used to quantitatively describe PAP depurination activity and PAP‐VPg interactions. PAP binds to VPg with high affinity (29.5 nM); the reaction is enthalpically driven and entropically favored. Further, VPg is a potent inhibitor of PAP depurination of RNA in wheat germ lysate, and competes with structured RNA derived from tobacco etch virus (TEV) for PAP binding. VPg may confer an evolutionary advantage by suppressing one of the plant defense mechanisms, and also suggests the possible use of this protein against the cytotoxic activity of RIPs.

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Section: Discussionsupporting

confidence: 69%

Section: Discussionsupporting

confidence: 69%

Section: Pokeweed Antiviral Protein (Pap)mentioning

confidence: 99%

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Inhibition of Pokeweed Antiviral Protein (PAP) by Turnip Mosaic Virus Genome-linked Protein (VPg)

Domashevskiy

Mizumoto

Goss

2012

Journal of Biological Chemistry

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“…An insertion at the proteolytic site between 6K2 and VPg (at Gly 1848 ) was deleterious. All insertions within the region corresponding to the domain interacting with the eukaryotic initiation factor eIF(iso)4E in Turnip mosaic potyvirus (Leonard et al 2000) were tolerated in PVA. The insertion at Met 1958 involved in vascular movement of PVA (Hämäläinen et al 2000) did not prevent propagation in protoplasts.…”

Section: Vpg Regionmentioning

confidence: 99%

Functional Genomics on Potato Virus A: Virus Genome-Wide Map of Sites Essential for Virus Propagation

Kekarainen¹,

Savilahti²,

Valkonen³

2002

Genome Res.

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Transposition-based in vitro insertional mutagenesis strategies provide promising new approaches for functional characterization of any cloned gene or genome region. We have extended the methodology and scope of such analysis to a complete viral genome. To map genome regions both essential and nonessential for Potato virus A propagation, we generated a genomic 15-bp insertion mutant library utilizing the efficient in vitro DNA transposition reaction of phage Mu. We then determined the proficiency of 1125 mutants to propagate in tobacco protoplasts by using a genetic footprinting strategy that simultaneously mapped the genomic insertion sites. Over 300 sites critical for virus propagation were identified, and many of them were located in positions previously not assigned to any viral functions. Many genome regions tolerated insertions indicating less important sites for virus propagation and thus pinpointed potential locations for further genome manipulation. The methodology described is applicable to a detailed functional analysis of any viral nucleic acid cloned as DNA and can be used to address many different processes during viral infection cycles

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“…The physical interaction between host eukaryotic initiation factor eIF4E or eIF(iso)4E and the viral genome-linked protein (VPg) is critical for viral infection by several members of the genus potyvirus (Wittmann et al, 1997;Leonard et al, 2000;Grzela et al, 2006;Miyoshi et al, 2006;Robaglia and Caranta, 2006). The major role of eIF4E in the host cell is initiating protein translation by allowing recognition and interaction with the cap structure of cellular mRNA.…”

Section: Introductionmentioning

confidence: 99%

Functional Dissection of Naturally Occurring Amino Acid Substitutions in eIF4E That Confers Recessive Potyvirus Resistance in Plants

et al. 2007

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Naturally existing variation in the eukaryotic translation initiation factor 4E (eIF4E) homolog encoded at the pvr1 locus in Capsicum results in recessively inherited resistance against several potyviruses. Previously reported data indicate that the physical interaction between Capsicum-eIF4E and the viral genome-linked protein (VPg) is required for the viral infection in the Capsicum-Tobacco etch virus (TEV) pathosystem. In this study, the potential structural role(s) of natural variation in the eIF4E protein encoded by recessive resistance alleles and their biological consequences have been assessed. Using highresolution three-dimensional structural models based on the available crystallographic structures of eIF4E, we show that the amino acid substitution G107R, found in many recessive plant virus resistance genes encoding eIF4E, is predicted to result in a substantial modification in the protein binding pocket. The G107R change was shown to not only be responsible for the interruption of VPg binding in planta but also for the loss of cap binding ability in vitro, the principal function of eIF4E in the host. Overexpression of the Capsicum-eIF4E protein containing the G107R amino acid substitution in Solanum lycopersicum indicated that this polymorphism alone is sufficient for the acquisition of resistance against several TEV strains.

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Complex Formation between Potyvirus VPg and Translation Eukaryotic Initiation Factor 4E Correlates with Virus Infectivity

Cited by 277 publications

References 71 publications

Inhibition of Pokeweed Antiviral Protein (PAP) by Turnip Mosaic Virus Genome-linked Protein (VPg)

Inhibition of Pokeweed Antiviral Protein (PAP) by Turnip Mosaic Virus Genome-linked Protein (VPg)

Functional Genomics on Potato Virus A: Virus Genome-Wide Map of Sites Essential for Virus Propagation

Functional Dissection of Naturally Occurring Amino Acid Substitutions in eIF4E That Confers Recessive Potyvirus Resistance in Plants

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