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Title: Structure of the Triatoma virus capsid

Abstract

The crystallographic structure of TrV shows specific morphological and functional features that clearly distinguish it from the type species of the Cripavirus genus, CrPV. The members of the Dicistroviridae family are non-enveloped positive-sense single-stranded RNA (+ssRNA) viruses pathogenic to beneficial arthropods as well as insect pests of medical importance. Triatoma virus (TrV), a member of this family, infects several species of triatomine insects (popularly named kissing bugs), which are vectors for human trypanosomiasis, more commonly known as Chagas disease. The potential use of dicistroviruses as biological control agents has drawn considerable attention in the past decade, and several viruses of this family have been identified, with their targets covering honey bees, aphids and field crickets, among others. Here, the crystal structure of the TrV capsid at 2.5 Å resolution is reported, showing that as expected it is very similar to that of Cricket paralysis virus (CrPV). Nevertheless, a number of distinguishing structural features support the introduction of a new genus (Triatovirus; type species TrV) under the Dicistroviridae family. The most striking differences are the absence of icosahedrally ordered VP4 within the infectious particle and the presence of prominent projections that surround the fivefold axis. Furthermore, the structure identifies a secondmore » putative autoproteolytic DDF motif in protein VP3, in addition to the conserved one in VP1 which is believed to be responsible for VP0 cleavage during capsid maturation. The potential meaning of these new findings is discussed.« less

Authors:
;  [1];  [2];  [3];  [4];  [5];  [6];  [7]; ;  [1];  [2];  [3];  [1]
  1. Laboratoire de Virologie Moléculaire et Structurale, CNRS, 1 Avenue de la Terrasse, 91198 Gif-sur-Yvette CEDEX (France)
  2. Fundación Biofísica Bizkaia, Barrio Sarriena S/N, 48940 Leioa, Bizkaia (FBB) (Spain)
  3. (UBF, CSIC, UPV/EHU), PO Box 644, 48080 Bilbao (Spain)
  4. U.N.S., San Juan 670 (8000) Bahía Blanca (Argentina)
  5. (8000) Bahía Blanca (Argentina)
  6. U.N.S., Avenida Alem 1253 (8000) Bahía Blanca (Argentina)
  7. Centro de Estudios Parasitológicos y de Vectores (CEPAVE-CCT, La Plata, CONICET-UNLP), Calle 2 No. 584 (1900) La Plata (Argentina)
Publication Date:
OSTI Identifier:
22347845
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section D: Biological Crystallography; Journal Volume: 69; Journal Issue: Pt 6; Other Information: PMCID: PMC3663122; PMID: 23695247; PUBLISHER-ID: mn5025; OAI: oai:pubmedcentral.nih.gov:3663122; Copyright (c) Squires et al. 2013; This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
Denmark
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; ATOMS; CLEAVAGE; COVERINGS; CRYSTAL STRUCTURE; CRYSTALS; POTENTIALS; PROTEINS; RESOLUTION; VECTORS

Citation Formats

Squires, Gaëlle, Pous, Joan, Agirre, Jon, Unidad de Biofísica, Rozas-Dennis, Gabriela S., U.N.S., Avenida Alem 1253, Costabel, Marcelo D., Marti, Gerardo A., Navaza, Jorge, Bressanelli, Stéphane, Guérin, Diego M. A., E-mail: diego.guerin@ehu.es, Unidad de Biofísica, and Rey, Felix A., E-mail: diego.guerin@ehu.es. Structure of the Triatoma virus capsid. Denmark: N. p., 2013. Web. doi:10.1107/S0907444913004617.
Squires, Gaëlle, Pous, Joan, Agirre, Jon, Unidad de Biofísica, Rozas-Dennis, Gabriela S., U.N.S., Avenida Alem 1253, Costabel, Marcelo D., Marti, Gerardo A., Navaza, Jorge, Bressanelli, Stéphane, Guérin, Diego M. A., E-mail: diego.guerin@ehu.es, Unidad de Biofísica, & Rey, Felix A., E-mail: diego.guerin@ehu.es. Structure of the Triatoma virus capsid. Denmark. doi:10.1107/S0907444913004617.
Squires, Gaëlle, Pous, Joan, Agirre, Jon, Unidad de Biofísica, Rozas-Dennis, Gabriela S., U.N.S., Avenida Alem 1253, Costabel, Marcelo D., Marti, Gerardo A., Navaza, Jorge, Bressanelli, Stéphane, Guérin, Diego M. A., E-mail: diego.guerin@ehu.es, Unidad de Biofísica, and Rey, Felix A., E-mail: diego.guerin@ehu.es. Sat . "Structure of the Triatoma virus capsid". Denmark. doi:10.1107/S0907444913004617.
@article{osti_22347845,
title = {Structure of the Triatoma virus capsid},
author = {Squires, Gaëlle and Pous, Joan and Agirre, Jon and Unidad de Biofísica and Rozas-Dennis, Gabriela S. and U.N.S., Avenida Alem 1253 and Costabel, Marcelo D. and Marti, Gerardo A. and Navaza, Jorge and Bressanelli, Stéphane and Guérin, Diego M. A., E-mail: diego.guerin@ehu.es and Unidad de Biofísica and Rey, Felix A., E-mail: diego.guerin@ehu.es},
abstractNote = {The crystallographic structure of TrV shows specific morphological and functional features that clearly distinguish it from the type species of the Cripavirus genus, CrPV. The members of the Dicistroviridae family are non-enveloped positive-sense single-stranded RNA (+ssRNA) viruses pathogenic to beneficial arthropods as well as insect pests of medical importance. Triatoma virus (TrV), a member of this family, infects several species of triatomine insects (popularly named kissing bugs), which are vectors for human trypanosomiasis, more commonly known as Chagas disease. The potential use of dicistroviruses as biological control agents has drawn considerable attention in the past decade, and several viruses of this family have been identified, with their targets covering honey bees, aphids and field crickets, among others. Here, the crystal structure of the TrV capsid at 2.5 Å resolution is reported, showing that as expected it is very similar to that of Cricket paralysis virus (CrPV). Nevertheless, a number of distinguishing structural features support the introduction of a new genus (Triatovirus; type species TrV) under the Dicistroviridae family. The most striking differences are the absence of icosahedrally ordered VP4 within the infectious particle and the presence of prominent projections that surround the fivefold axis. Furthermore, the structure identifies a second putative autoproteolytic DDF motif in protein VP3, in addition to the conserved one in VP1 which is believed to be responsible for VP0 cleavage during capsid maturation. The potential meaning of these new findings is discussed.},
doi = {10.1107/S0907444913004617},
journal = {Acta Crystallographica. Section D: Biological Crystallography},
number = Pt 6,
volume = 69,
place = {Denmark},
year = {Sat Jun 01 00:00:00 EDT 2013},
month = {Sat Jun 01 00:00:00 EDT 2013}
}