Crystallographic and cryo EM analysis of virion-receptor interactions.

M. G. Rossmann, N. H. Olson, Prasanna Kolatkar, M. A. Oliveira, R. H. Cheng, J. M. Greve, A. McClelland, T. S. Baker

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Abstract

Cryoelectron microscopy has been used to determine the first structure of a virus when complexed with its glycoprotein cellular receptor. Human rhinovirus 16 (HRV16) complexed with the two amino-terminal, immunoglobulin-like domains of the intercellular adhesion molecule-1 (ICAM-1) shows that ICAM-1 binds into the 12 A deep "canyon" on the surface of the virus. This is consistent with the prediction that the viral receptor attachment site lies in a cavity inaccessible to the host's antibodies. The atomic structures of HRV14 and CD4, homologous to HRV16 and ICAM-1, showed excellent correspondence with observed density, thus establishing the virus-receptor interactions.

Original languageEnglish
Pages (from-to)531-541
Number of pages11
JournalArchives of virology. Supplementum
Volume9
Publication statusPublished - 1 Jan 1994
Externally publishedYes

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ASJC Scopus subject areas

  • Immunology and Microbiology(all)

Cite this

Rossmann, M. G., Olson, N. H., Kolatkar, P., Oliveira, M. A., Cheng, R. H., Greve, J. M., McClelland, A., & Baker, T. S. (1994). Crystallographic and cryo EM analysis of virion-receptor interactions. Archives of virology. Supplementum, 9, 531-541.