Structure of the Triatoma virus capsid

• Autores: Squires, G.; Pous, J.; Agirre, J.; Rozas-Dennis, G.S.; Costabel, Marcelo D.; Martí, Gerardo Aníbal; Navaza, Jorge; Bressanelli, S.; Guérin, D. M. A.; Rey, F. A.
• Año de publicación: 2013
• Idioma: inglés
• Tipo de recurso: artículo
• Materia: Ciencias Naturales; Cripavirus; Dicistroviridae; Triatoma virus; TrV; virus structure; X-ray crystallography
• Institución: Universidad Nacional de La Plata

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 14;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.
Centro de Estudios Parasitológicos y de Vectores