Crystallographic and cryo EM analysis of virion-receptor interactions.

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

doi:10.1007/978-3-7091-9326-6_51

Crystallographic and cryo EM analysis of virion-receptor interactions.

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

^*Corresponding author for this work

Purdue University

Research output: Contribution to journal › Article › peer-review

16 Citations (Scopus)

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 language	English
Pages (from-to)	531-541
Number of pages	11
Journal	Archives of virology. Supplementum
Volume	9
DOIs	https://doi.org/10.1007/978-3-7091-9326-6_51
Publication status	Published - 1994
Externally published	Yes

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title = "Crystallographic and cryo EM analysis of virion-receptor interactions.",

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.",

author = "Rossmann, \{M. G.\} and Olson, \{N. H.\} and Kolatkar, \{P. R.\} and Oliveira, \{M. A.\} and Cheng, \{R. H.\} and Greve, \{J. M.\} and A. McClelland and Baker, \{T. S.\}",

year = "1994",

doi = "10.1007/978-3-7091-9326-6\_51",

language = "English",

volume = "9",

pages = "531--541",

journal = "Archives of virology. Supplementum",

issn = "0939-1983",

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TY - JOUR

T1 - Crystallographic and cryo EM analysis of virion-receptor interactions.

AU - Rossmann, M. G.

AU - Olson, N. H.

AU - Kolatkar, P. R.

AU - Oliveira, M. A.

AU - Cheng, R. H.

AU - Greve, J. M.

AU - McClelland, A.

AU - Baker, T. S.

PY - 1994

Y1 - 1994

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/0028252183

U2 - 10.1007/978-3-7091-9326-6_51

DO - 10.1007/978-3-7091-9326-6_51

M3 - Article

C2 - 7913361

AN - SCOPUS:0028252183

SN - 0939-1983

VL - 9

SP - 531

EP - 541

JO - Archives of virology. Supplementum

JF - Archives of virology. Supplementum

ER -

Crystallographic and cryo EM analysis of virion-receptor interactions.

Abstract

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