Intrinsic Disorder in Genome‐Linked Viral Proteins VPgs of Potyviruses

Chroboczek, Jadwiga; Hébrard, Eugénie; Mäkinen, Kristiina; Michon, Thierry; Rantalainen, Kimmo

doi:10.1002/9781118135570.ch11

Cited by 3 publications

(3 citation statements)

References 110 publications

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“…S1b) seem to exclude the possibility that the differences observed could be artefactual. However, the higher binding observed with the LMV-E VPg could be due either to its higher CI-binding efficiency or to a higher ability to form dimers (Chroboczek et al , 2012) under the conditions used.…”

Section: Discussionmentioning

confidence: 99%

The C terminus of lettuce mosaic potyvirus cylindrical inclusion helicase interacts with the viral VPg and with lettuce translation eukaryotic initiation factor 4E

Tavert-Roudet

Abdul-Razzak

Doublet

et al. 2012

Journal of General Virology

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Recessive resistance to lettuce mosaic virus (LMV) is conferred in lettuce by the mo1 gene, encoding the eukaryotic translation initiation factor 4E (eIF4E). The C terminus of the viral cylindrical inclusion helicase (CI-Cter), together with the VPg, is involved directly in overcoming mo1 resistance. In this study, recombinant LMV VPg and CI-Cter proteins from wild-type or resistance-breaking isolates were expressed and purified from Escherichia coli. The allelic forms of eIF4E from susceptible or resistant lettuce cultivars were produced similarly and these proteins were used in ELISA-based assays to demonstrate the in vitro binding of the various forms of LMV CI-Cter to both lettuce eIF4E and LMV VPg proteins. All combinations tested displayed significant and specific interactions, and the interaction between the C-terminal part of the LMV CI and eIF4E was confirmed in vivo in bimolecular fluorescence complementation assays. Higher interaction signals for both CI-eIF4E and CI-VPg were observed for LMV-E, indicating that the eIF4E interaction network involving CI and VPg appears to be stronger in the case of this resistance-breaking isolate. This could suggest the need for a minimal interaction threshold for infection success in resistant lettuce, but more precise measurement of the interaction parameters linking eIF4E, VPg and CI is needed in order to reinforce such a hypothesis.

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Section: Discussionmentioning

confidence: 99%

The C terminus of lettuce mosaic potyvirus cylindrical inclusion helicase interacts with the viral VPg and with lettuce translation eukaryotic initiation factor 4E

Tavert-Roudet

Abdul-Razzak

Doublet

et al. 2012

Journal of General Virology

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“…It was previously deduced from hydrodynamic parameters determination that VPg behaves as a pre-molten globule [34]. This type of protein possesses loosely packed cores involving secondary structures interspaced with disordered regions [35].…”

Section: Discussionmentioning

confidence: 99%

Comparative analysis of mutational robustness of the intrinsically disordered viral protein VPg and of its interactor eIF4E

Walter

Charon

et al. 2019

PLoS ONE

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Conformational intrinsic disorder is a feature present in many virus proteins. Intrinsically disordered regions (IDRs) have weaker structural requirement than ordered regions and mutations in IDRs could have a lower impact on the virus fitness. This could favor its exploration of adaptive solutions. The potyviral protein VPg contains IDRs with determinants for adaptation to its host plant. To experimentally assess whether IDRs are more resistant to mutations than ordered regions, the biologically relevant interaction between mutant libraries of both VPg and the eukaryotic translation initiation factor 4E (eIF4E) and their respective wild type partner was examined using yeast two hybrid assay. Our data shows that VPg is significantly more robust to mutations than eIF4E and as such belongs to a particular class of intrinsically disordered proteins. This result is discussed from the standpoint of IDRs involvement in the virus adaptive processes.

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“…The multifunctional Viral genome linked protein (VPg) participates to several of them, and constitutes a major pathogenicity factor in potyviruses ( Jiang and Laliberté 2011 ; Elena and Rodrigo 2012 ). The VPg has been experimentally characterized as intrinsically disordered in various potyviruses ( Grzela et al 2008 ; Rantalainen et al 2008 ; Chroboczek et al 2012 ). VPg IDRs are maintained within the whole Potyvirus genus, despite a high level of amino acid polymorphism, strongly suggesting a functional role of these regions in the virus fitness ( Hébrard et al 2009 ; Charon et al 2016 ).…”

Section: Introductionmentioning

confidence: 99%

First Experimental Assessment of Protein Intrinsic Disorder Involvement in an RNA Virus Natural Adaptive Process

Charon

Barra

Walter

et al. 2017

Molecular Biology and Evolution

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Intrinsic disorder (ID) in proteins is defined as a lack of stable structure in physiological conditions. Intrinsically disordered regions (IDRs) are highly abundant in some RNA virus proteomes. Low topological constraints exerted on IDRs are expected to buffer the effect of numerous deleterious mutations and could be related to the remarkable adaptive potential of RNA viruses to overcome resistance of their host. To experimentally test this hypothesis in a natural pathosystem, a set of four variants of Potato virus Y (PVY; Potyvirus genus) containing various ID degrees in the Viral genome-linked (VPg) protein, a key determinant of potyvirus adaptation, was designed. To estimate the ID contribution to the VPg-based PVY adaptation, the adaptive ability of the four PVY variants was monitored in the pepper host (Capsicum annuum) carrying a recessive resistance gene. Intriguingly, the two mutants with the highest ID content displayed a significantly higher ability to restore infection in the resistant host, whereas the less intrinsically disordered mutant was unable to restore infection. The role of ID on virus adaptation may be due either to a larger exploration of evolutionary pathways or the minimization of fitness penalty caused by resistance-breaking mutations. This pioneering study strongly suggests the positive impact of ID in an RNA virus adaptive capacity.

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Intrinsic Disorder in Genome‐Linked Viral Proteins VPgs of Potyviruses

Cited by 3 publications

References 110 publications

The C terminus of lettuce mosaic potyvirus cylindrical inclusion helicase interacts with the viral VPg and with lettuce translation eukaryotic initiation factor 4E

The C terminus of lettuce mosaic potyvirus cylindrical inclusion helicase interacts with the viral VPg and with lettuce translation eukaryotic initiation factor 4E

Comparative analysis of mutational robustness of the intrinsically disordered viral protein VPg and of its interactor eIF4E

First Experimental Assessment of Protein Intrinsic Disorder Involvement in an RNA Virus Natural Adaptive Process

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