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

Rubén Sánchez-Eugenia¹, Fernando Méndez², Jailson F B Querido^3,4,1

¹Unidad de Biofísica (CSIC, UPV/EHU), Barrio Sarriena S/N, 48940 Leioa, Bizkaia, Spain.

The Journal of General Virology

|October 12, 2014

Summary

Triatoma virus (TrV) assembly requires coexpression of non-structural (NS) and structural (P1) proteins. This process forms virus-like particles (VLPs) and a novel, larger intermediate, differing from related picornaviruses.

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Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus

Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus

Published on: July 27, 2021

Area of Science:

Virology
Molecular Biology
Structural Biology

Background:

Dicistrovirus particle structure is well-characterized, but their morphogenetic pathways remain largely unknown.
Triatoma virus (TrV), a Cripavirus, infects insects and transmits Trypanosoma cruzi, the cause of Chagas disease.

Purpose of the Study:

To investigate the expression and proteolytic processing of Triatoma virus (TrV) non-structural (NS) and structural (P1) polyproteins.
To elucidate the role of NS and P1 polyproteins in TrV assembly and virus-like particle (VLP) formation.

Main Methods:

Established a baculovirus-based expression system for TrV NS and P1 polyproteins.
Analyzed the proteolytic processing of TrV polyprotein precursors.
Characterized the morphology and protein composition of assembled structures.

Main Results:

Proteolytic processing of the P1 polyprotein is dependent on the coexpression of the NS polyprotein.
Coexpression of NS and P1 polyproteins results in the assembly of TrV virus-like particles (VLPs) similar to natural empty capsids.
Unprocessed P1 polypeptide forms larger, quasi-spherical structures, suggesting a novel morphogenetic intermediate.

Conclusions:

TrV assembly requires the concerted action of NS and P1 polyproteins.
A previously undescribed morphogenetic intermediate in TrV assembly was identified.
These findings suggest significant differences in assembly pathways between Dicistroviridae and Picornaviridae families.