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Correction: Structural Insights into Viral Determinants of Nematode Mediated Grapevine fanleaf virus Transmission
- Source :
- PLoS Pathogens, PLoS Pathogens, Public Library of Science, 2017, 13 (3), pp.e1006268. ⟨10.1371/journal.ppat.1006268⟩, PLoS Pathogens, 2017, 13 (3), pp.e1006268. ⟨10.1371/journal.ppat.1006268⟩, PLoS Pathogens, Vol 13, Iss 3, p e1006268 (2017)
- Publication Year :
- 2017
- Publisher :
- HAL CCSD, 2017.
-
Abstract
- Many animal and plant viruses rely on vectors for their transmission from host to host. Grapevine fanleaf virus (GFLV), a picorna-like virus from plants, is transmitted specifically by the ectoparasitic nematode Xiphinema index. The icosahedral capsid of GFLV, which consists of 60 identical coat protein subunits (CP), carries the determinants of this specificity. Here, we provide novel insight into GFLV transmission by nematodes through a comparative structural and functional analysis of two GFLV variants. We isolated a mutant GFLV strain (GFLV-TD) poorly transmissible by nematodes, and showed that the transmission defect is due to a glycine to aspartate mutation at position 297 (Gly297Asp) in the CP. We next determined the crystal structures of the wild-type GFLV strain F13 at 3.0 Å and of GFLV-TD at 2.7 Å resolution. The Gly297Asp mutation mapped to an exposed loop at the outer surface of the capsid and did not affect the conformation of the assembled capsid, nor of individual CP molecules. The loop is part of a positively charged pocket that includes a previously identified determinant of transmission. We propose that this pocket is a ligand-binding site with essential function in GFLV transmission by X. index. Our data suggest that perturbation of the electrostatic landscape of this pocket affects the interaction of the virion with specific receptors of the nematode's feeding apparatus, and thereby severely diminishes its transmission efficiency. These data provide a first structural insight into the interactions between a plant virus and a nematode vector.
- Subjects :
- lcsh:Immunologic diseases. Allergy
Nematoda
[SDV]Life Sciences [q-bio]
Nepovirus
Static Electricity
Immunology
[SDV.BBM.BM] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology
Microbiology
Plant Viruses
03 medical and health sciences
Capsid
X-Ray Diffraction
Sequence Analysis, Protein
Virology
Genetics
[SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology
Animals
[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology
Protein Structure, Quaternary
lcsh:QH301-705.5
Molecular Biology
ComputingMilieux_MISCELLANEOUS
Plant Diseases
030304 developmental biology
0303 health sciences
030302 biochemistry & molecular biology
Correction
[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology
[SDV] Life Sciences [q-bio]
lcsh:Biology (General)
Amino Acid Substitution
Mutation
RNA, Viral
Capsid Proteins
Parasitology
lcsh:RC581-607
Sequence Alignment
Subjects
Details
- Language :
- English
- ISSN :
- 15537366 and 15537374
- Database :
- OpenAIRE
- Journal :
- PLoS Pathogens, PLoS Pathogens, Public Library of Science, 2017, 13 (3), pp.e1006268. ⟨10.1371/journal.ppat.1006268⟩, PLoS Pathogens, 2017, 13 (3), pp.e1006268. ⟨10.1371/journal.ppat.1006268⟩, PLoS Pathogens, Vol 13, Iss 3, p e1006268 (2017)
- Accession number :
- edsair.doi.dedup.....384e69406df95285a9d4d32f82557403
- Full Text :
- https://doi.org/10.1371/journal.ppat.1006268⟩