Noroviruses and rotaviruses recognize highly polymorphic human histo-blood group antigens as receptors or ligands for attachment through conserved and variable binding regions.
Noroviruses and rotaviruses utilize diverse recognition patterns to bind human histo-blood group antigens, highlighting functional adaptations of these viruses to host receptors.
Noroviruses (NoVs) and rotaviruses (RVs), the two most important causes of viral acute gastroenteritis, are found to recognise histo-blood group antigens (HBGAs) as receptors or ligands for attachment. Human HBGAs are highly polymorphic containing ABO, secretor and Lewis antigens. In addition, both NoVs and RVs are highly diverse in how they recognise these HBGAs. Structural analysis of the HBGA-binding interfaces of NoVs revealed a conserved central binding pocket (CBP) interacting with a common major binding saccharide (MaBS) of HBGAs and a variable surrounding region interacting with additional minor binding saccharides. The conserved CBP indicates a strong selection of NoVs by the host HBGAs, whereas the variable surrounding region explains the diverse recognition patterns of different HBGAs by NoVs and RVs as functional adaptations of the viruses to human HBGAs. Diverse recognition of HBGAs has also been found in bacterial pathogen Helicobacter pylori. Thus, exploratory research into whether such diverse recognitions also occur for other viral and bacterial pathogens that recognise HBGAs is warranted.
Tan et al. (Wed,) conducted a review in Viral acute gastroenteritis. Noroviruses and rotaviruses recognize highly polymorphic human histo-blood group antigens as receptors or ligands for attachment through conserved and variable binding regions.