Chemical Shift Perturbations Reflect Bile Acid Binding to Norovirus Coat Protein - Recognition Comes in Different Flavors.

Chemical Shift Perturbations Reflect Bile Acid Binding to Norovirus Coat Protein - Recognition Comes in Different Flavors. Chembiochem. 2019 Oct 23;: Authors: Peters T, Creutznacher R, Schulze E, Wallmann G, Stein M, Mallagaray A Abstract Bile acids have been reported as important co-factors promoting human and murine Norovirus (NoV) infections in cell culture. The underlying mechanisms are not resolved. Using chemical shift perturbation (CSP) NMR experiments we have identified a low-affinity bile acid binding site of a human GII.4 NoV strain. Long-timescale MD simulations reveal the formation of a ligand-accessible binding pocket of flexible shape, allowing the formation of stable viral coat protein:bile acid complexes in agreement with experimental CSP data. CSP NMR experiments also show that this mode of bile acid binding has minor influence on binding of histo blood group antigens and  vice versa . STD NMR experiments probing binding of bile acids to virus like particles of seven different strains suggest that low-affinity bile acid-binding is a common feature of human NoV and, therefore, should be important for understanding the role of bile acids as co-factors in NoV infection. PMID: 31644826 [PubMed - as supplied by publisher]
Source: Chembiochem - Category: Biochemistry Authors: Tags: Chembiochem Source Type: research