Abstract

Noroviruses are the main cause for acute gastroenteritis disease. They infect the host cell via interaction with HGBA receptors on the cell surface. Virus makes complex with cell surface receptors through its capsid protein VP1 to enter the cell. Although the protein has been successfully crystallized in the presence of some common glycans, the dynamic change in the protein structure when interacting with sugar moieties has yet to be fully elucidated. This is critically important since it leads to understanding the protein’s recognition mechanism of HBGAs and develop therapeutic strategies against the gastroenteritis disease. Here, we computationally assessed the dynamic features of wild type VP1 envelope protein to get insights into the interactions that can be important for virus infectivity. We have found that the binding of sugar moiety does not cause noticeable dynamic changes in the binding region. However, interestingly, a drastic change occurs in a distant loop lying at the residue numbers of 395-400, which might be indication of an allosteric effect.