Key result
Intergenotypic sequence differences influence how VP1 and VP2 functionally engage each other to mediate RNA synthesis in vitro, increasing understanding of RVA protein-level diversity.
The study increases understanding of RVA protein-level diversity and VP1-VP2 binding interfaces important for viral replication.
May guide antiviral targeting of VP1-VP2 interfaces; leaves open in vivo relevance of intergenotypic effects.
Group A rotaviruses (RVAs) are widespread in nature, infecting numerous mammalian and avian hosts and causing severe gastroenteritis in human children. RVAs are classified using a system that assigns a genotype to each viral gene according to its nucleotide sequence. To date, 22 genotypes have been described for the gene encoding the viral polymerase (VP1), and 20 genotypes have been described for the gene encoding the core shell protein (VP2). Here, we analyzed if/how the VP1 and VP2 proteins encoded by the known RVA genotypes differ from each other in their sequences. We also used a biochemical approach to test whether the intergenotypic sequence differences influenced how VP1 and VP2 functionally engage each other to mediate RNA synthesis in a test tube. This work is important because it increases our understanding of RVA protein-level diversity and raises new ideas about the VP1-VP2 binding interface(s) that is important for viral replication.
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Steger et al. (2018) studied Group A rotavirus. Biochemical analysis of VP1 and VP2 proteins was evaluated on Intergenotypic sequence differences and functional engagement of VP1 and VP2. Intergenotypic sequence differences influence how VP1 and VP2 functionally engage each other to mediate RNA synthesis in vitro, increasing understanding of RVA protein-level diversity.
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