Triatoma virus (TrV) is a member of the insect virus family Dicistroviridae and consists of a small, non-enveloped capsid that encloses its positive-sense ssRNA genome. TrV virus like particles (VLPs) have been previously obtained after genome release from native virions (1). The empty TrV capsid maintains a protein shell thickness and size identical to that in full virions. The capsid polyprotein has also been obtained in a baculovirus-based expression model (2). Due to many advantages that E. coli protein expression could represent versus the mentioned methods and to the variety of nanotechnological applications of VLPs, we are optimizing the expression in bacteria, purification and in vitro assembly of individual viral subunits. As previous results suggested the possibility that the coexpression of both TrV cistrons (structural and non-structural ORFs) might lead to the assembly of TrV-derived VLPs, we are also coexpressing the polyprotein precursor and protease in bacteria. Virus like particles (VLP) self-assembly in vitro from protein subunits have been assayed under different conditions (protein concentration, temperature, pH, ionic strength, presence of macromolecular crowding agents or biopolymers). The development and redesign of virus-based platforms for biomedical and biotechnological applications will benefit from easily obtained and modified recombinant viral proteins.

Póster presentado al 8th International Iberian Biophysics Congress celebrado en Bilbao los días 20 y 21 de junio de 2022.