Identification of a recombinant GII.13[P21] norovirus strain: molecular dynamic simulations indicate that gene mutations shifted its spectrum of binding to host receptor glycans.

Human norovirus is a pervasive pathogen that causes global outbreaks of viral gastroenteritis. Previous studies have suggested that histo-blood group antigens (HBGAs) can interact with human norovirus, facilitating its entry of host cells and significantly affecting its evolution. In this study, the complete genome sequence of recombinant GII.13[P21] norovirus from fecal samples was analyzed. Molecular dynamics simulations of GII.13 norovirus P proteins from 1978 to 2019 showed changes in their capacity to bind to HBGAs. Initially, GII.13 proteins bound A or B/H-type HBGAs, but subsequent mutations resulted in a loss of this binding capacity, favoring binding to the HBGA type I precursor (Lewis c) over A or B/H and Lewis antigens.