Abstract
Measles virus is a highly pathogenic virus that infects roughly 20 million people per year. We report here the crystal structure of the measles virus hemagglutinin, the surface glycoprotein responsible for the binding of measles virus to its host cell receptors. Although the protein lacks neuraminidase activity, its structure resembles a 'dead' neuraminidase fold, presenting spatially distinct receptor-binding sites for its receptors CD46 and SLAM.
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Acknowledgements
We thank M. Oldstone, L. Martin and B. Hahm (The Scripps Research Institute) for complementary DNA encoding MVH. L.A.C. is supported by a US National Science Foundation graduate research fellowship. K.C.G. is supported by the Howard Hughes Medical Institute and the US National Institutes of Health.
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Supplementary Figures 1–3, Supplementary Table 1, Supplementary Methods (PDF 1417 kb)
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Colf, L., Juo, Z. & Garcia, K. Structure of the measles virus hemagglutinin. Nat Struct Mol Biol 14, 1227–1228 (2007). https://doi.org/10.1038/nsmb1342
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DOI: https://doi.org/10.1038/nsmb1342
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