Introduction

Rotavirus (RV) is a highly infectious pathogen responsible for approximately 200,000 child fatalities annually worldwide. Symptoms of the infection include diarrhea, vomiting, fever and abdominal pain. Certain RV strains, including G3P[10] from bat species, exhibit zoonotic potential, enabling transmission between animal and human hosts. The structural characterization of RV binding mechanisms is essential for understanding viral host adaptation and evolution. RV consists of 11 double-stranded RNA segments encoding six structural and six non-structural viral proteins. Host cell attachment is mediated by VP4, which undergoes proteolytic cleavage into VP5 and VP8, enhancing viral infectivity (Figure 2). 

The primary objective of this research is to characterize the structural binding mechanism of VP8, as this domain plays a critical role in host recognition and viral potency. Glycan-binding assays and structural analyses are being conducted to determine VP8-host interactions. Evolutionary relationships between RV strains are inferred based on similarities in glycan recognition patterns. Future statistical analyses will involve comparative binding affinity assays to quantify VP8-glycan interactions across different host species. Initial observations suggest variations in VP8 binding specificity, which may contribute to the ability of RV to cross species barriers. Findings from this study will contribute to the broader understanding of RV zoonosis and potential risks associated with emerging viral strains.