Structure of the<i>Triatoma virus</i>capsid

Squires, G.; Pous, Joan; Agirre, Jon; Rozas-Dennis, Gabriela S.; Costabel, Marcelo Daniel; Martí, Gerardo A.; Navaza, Jorge; Bressanelli, Stéphane; Guérin, Diego M. A.; Rey, F.A.

doi:10.1107/s0907444913004617

Cited by 37 publications

(102 citation statements)

References 55 publications

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“…Therefore, the structure of the SBPV empty particle together with the negative results of the liposome lysis experiment described above indicate that the N terminus of SBPV VP1 is unlikely to interact with membranes. The genome release of TrV from the family Dicistroviridae does not involve structural changes to the capsid before the genome release (13). However, the empty Comparison of interactions of residues around threefold symmetry axis of the capsid in native SBPV (E) and empty low-pH particle (F).…”

Section: Genome Release Is Associated With Formation Of Pores At Thrementioning

confidence: 99%

“…VP1 subunits are clustered around fivefold axes, and VP2 and VP3 form hetero-hexamers around icosahedral threefold axes. Unlike in the related picornaviruses and dicistroviruses, capsid protein VP3 of SBPV contains a C-terminal extension that folds into a globular protruding (P) domain positioned at the virion surface (10)(11)(12)(13). At neutral pH, the P domains form "crowns" on the virion surface around each fivefold axis of the virus.…”

mentioning

confidence: 99%

“…Cryo-EM reconstructions of genome-containing and empty TrV particles determined to resolutions of 15-22 Å demonstrated that the TrV empty particles are very similar to the native virions. After the genome release, the empty TrV capsids rapidly disassemble into pentamers (13).…”

mentioning

confidence: 99%

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Cryo-EM study of slow bee paralysis virus at low pH reveals iflavirus genome release mechanism

Kalynych

Füzik

Přidal

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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Viruses from the family Iflaviridae are insect pathogens. Many of them, including slow bee paralysis virus (SBPV), cause lethal diseases in honeybees and bumblebees, resulting in agricultural losses. Iflaviruses have nonenveloped icosahedral virions containing single-stranded RNA genomes. However, their genome release mechanism is unknown. Here, we show that low pH promotes SBPV genome release, indicating that the virus may use endosomes to enter host cells. We used cryo-EM to study a heterogeneous population of SBPV virions at pH 5.5. We determined the structures of SBPV particles before and after genome release to resolutions of 3.3 and 3.4 Å, respectively. The capsids of SBPV virions in low pH are not expanded. Thus, SBPV does not appear to form "altered" particles with pores in their capsids before genome release, as is the case in many related picornaviruses. The egress of the genome from SBPV virions is associated with a loss of interpentamer contacts mediated by N-terminal arms of VP2 capsid proteins, which result in the expansion of the capsid. Pores that are 7 Å in diameter form around icosahedral threefold symmetry axes. We speculate that they serve as channels for the genome release. Our findings provide an atomic-level characterization of the genome release mechanism of iflaviruses.electron microscopy | uncoating | honeybee | structure | virus

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Section: Genome Release Is Associated With Formation Of Pores At Thrementioning

confidence: 99%

mentioning

confidence: 99%

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Cryo-EM study of slow bee paralysis virus at low pH reveals iflavirus genome release mechanism

Kalynych

Füzik

Přidal

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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“…These capsids are naked icosahedrons (T53 symmetry) built by 60 copies of each of the three major structural proteins VP1-3 (all folded with a jelly roll core). Both TrV and CrPV capsids are quite similar (Squires et al, 2013), with the location of the VP4 peptide being the main structural difference between them (Tate et al, 1999;Squires et al, 2013). Characterization of the TrV capsid disassembly and genome release allowed us to propose a novel RNA-release mechanism for this virus Snijder et al, 2013) that differs from those proposed for members of the Picornaviridae family, i.e.…”

Section: Introductionmentioning

confidence: 99%

“…The capsid structures of two dicistroviruses, TrV and Cricket paralysis virus (CrPV), have been characterized at the atomic level (Squires et al, 2013;Tate et al, 1999). These capsids are naked icosahedrons (T53 symmetry) built by 60 copies of each of the three major structural proteins VP1-3 (all folded with a jelly roll core).…”

Section: Introductionmentioning

confidence: 99%

Triatoma virus structural polyprotein expression, processing and assembly into virus-like particles

Sánchez-Eugenia

Méndez

Querido

et al. 2015

Journal of General Virology

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In contrast to the current wealth of structural information concerning dicistrovirus particle structure, very little is known about their morphogenetic pathways. Here, we describe the expression of the two ORFs encoded by the Triatoma virus (TrV) genome. TrV, a member of the Cripavirus genus of the Dicistroviridae family, infects blood-sucking insects belonging to the Triatominae subfamily that act as vectors for the transmission of Trypanosoma cruzi, the aetiological agent of the Chagas disease. We have established a baculovirus-based model for the expression of the NS (non-structural) and P1 (structural) polyproteins. A preliminary characterization of the proteolytic processing of both polyprotein precursors has been performed using this system. We show that the proteolytic processing of the P1 polyprotein is strictly dependent upon the coexpression of the NS polyprotein, and that NS/P1 coexpression leads to the assembly of virus-like particles (VLPs) exhibiting a morphology and a protein composition akin to natural TrV empty capsids. Remarkably, the unprocessed P1 polypeptide assembles into quasispherical structures conspicuously larger than VLPs produced in NS/P1-coexpressing cells, likely representing a previously undescribed morphogenetic intermediate. This intermediate has not been found in members of the related Picornaviridae family currently used as a model for dicistrovirus studies, thus suggesting the existence of major differences in the assembly pathways of these two virus groups.

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Alkalinization of Icosahedral Non-enveloped Viral Capsid Interior Through Proton Channeling

Branda

Guérin

2019

Advances in Experimental Medicine and Biology

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Structure of theTriatoma viruscapsid

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.

Cited by 37 publications

References 55 publications

Cryo-EM study of slow bee paralysis virus at low pH reveals iflavirus genome release mechanism

Cryo-EM study of slow bee paralysis virus at low pH reveals iflavirus genome release mechanism

Triatoma virus structural polyprotein expression, processing and assembly into virus-like particles

Alkalinization of Icosahedral Non-enveloped Viral Capsid Interior Through Proton Channeling

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