Computational analysis of the Immunogenic regions at the TrV capsid

PORASSO, RODOLFO D.; SERGIO PANTANO; DIEGO GUERIN; MARIA MARTA BRANDA

Bilbao

Congreso; 8th International Iberian Biophysics Congress; 2022

Virus-like particles (VLPs) are formed by the self-assembly of capsid proteins from many viruses. Due to the high immunogenic stimulation property, VLPs have been used as vaccine platforms by carrying heterologous antigens, i.e. epitopes from different pathogens or tumor cells. One of the main issues in designing VLP-based vaccines is to decide the point of insertion and the number of epitopes to carry by the VLP. In this sense, computational analysis of the VLPs' protein structure and amino acid sequences, are very useful tools in vaccine design. In this work we study triatoma virus VLP. We combine Molecular Dynamics (MD) simulation, and predictions of the proteasome cleavage and toxicity, to find the number of regions in the VLP and their length, that are more adequate to be substituted by foreign peptides. Our hypothesis stems from studies done on different human virus VLPs1, which found that low mobility protein regions have greater immunogenicity than regions of high mobility. The MD calculations indicate that TrV-VLPs have at least 17 stretches of low mobility, that combined with cleavage and toxicity analyses, result that in TrV-VLPs.