Structure of measles virus hemagglutinin bound to its epithelial receptor nectin-4
Zhang, X., Lu, G., Qi, J., Li, Y., He, Y., Xu, X., Shi, J., Zhang, C.W., Yan, J., Gao, G.F.(2013) Nat Struct Mol Biol 20: 67-72
- PubMed: 23202587
- DOI: https://doi.org/10.1038/nsmb.2432
- Primary Citation of Related Structures:
4GJT - PubMed Abstract:
Measles virus is a major public health concern worldwide. Three measles virus cell receptors have been identified so far, and the structures of the first two in complex with measles virus hemagglutinin (MV-H) have been reported. Nectin-4 is the most recently identified receptor in epithelial cells, and its binding mode to MV-H remains elusive. In this study, we solved the structure of the membrane-distal domain of human nectin-4 in complex with MV-H. The structure shows that nectin-4 binds the MV-H β4-β5 groove exclusively via its N-terminal IgV domain; the contact interface is dominated by hydrophobic interactions. The binding site in MV-H for nectin-4 also overlaps extensively with those of the other two receptors. Finally, a hydrophobic pocket centered in the β4-β5 groove is involved in binding to all three identified measles virus receptors, representing a potential target for antiviral drugs.
Organizational Affiliation:
CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.