Unravelling aggregation propensity of rotavirus A VP6 expressed as E. coli inclusion bodies through in silico prediction.

ABSTRACT: The inner capsid protein of rotavirus, VP6, emerges as a promising candidate for next-generation vaccines against rotaviruses owing to its abundance in virion particles and high conservation. However, the formation of inclusion bodies during prokaryotic VP6 expression poses a significant hurdle to rotavirus research and applications. Here, we employed experimental and computational approaches to investigate inclusion body formation and aggregation-prone regions (APRs). Heterologous recombinant VP6 expression in Escherichia coli BL21(DE3) cells resulted in inclusion body formation, confirmed by transmission electron microscopy revealing amorphous aggregates. Thioflavin T assay demonstrated incubation temperature-dependent aggregation of VP6 inclusion bodies. Computational predictions of APR

SUBMITTER: Kuri PR 

PROVIDER: S-EPMC11399443 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature