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Structural Insights into Viral Determinants of Nematode Mediated
Transmission


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.


Vyšlo v časopise: Structural Insights into Viral Determinants of Nematode Mediated Transmission. PLoS Pathog 7(5): e32767. doi:10.1371/journal.ppat.1002034
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.ppat.1002034

Souhrn

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.


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