Interaction of coxsackievirus B3 with the full length coxsackievirus-adenovirus receptor

Yongning He; Paul R. Chipman; Jason Howitt; Carol M. Bator; Michael A. Whitt; Timothy S. Baker; Richard J. Kuhn; Carl W. Anderson; Paul Freimuth; Michael G. Rossmann

doi:10.1038/nsb1001-874

Interaction of coxsackievirus B3 with the full length coxsackievirus-adenovirus receptor

Yongning He, Paul R. Chipman, Jason Howitt, Carol M. Bator, Michael A. Whitt, Timothy S. Baker, Richard J. Kuhn, Carl W. Anderson, Paul Freimuth, Michael G. Rossmann

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

190 Scopus citations

Abstract

Group B coxsackieviruses (CVB) utilize the coxsackievirus-adenovirus receptor (CAR) to recognize host cells. CAR is a membrane protein with two Ig-like extracellular domains (D1 and D2), a transmembrane domain and a cytoplasmic domain. The three-dimensional structure of coxsackievirus B3 (CVB3) in complex with full length human CAR and also with the D1D2 fragment of CAR were determined to ∼22 Å resolution using cryo-electron microscopy (cryo-EM). Pairs of transmembrane domains of CAR associate with each other in a detergent cloud that mimics a cellular plasma membrane. This is the first view of a virus-receptor interaction at this resolution that includes the transmembrane and cytoplasmic portion of the receptor. CAR binds with the distal end of domain D1 in the canyon of CVB3, similar to how other receptor molecules bind to entero- and rhinoviruses. The previously described interface of CAR with the adenovirus knob protein utilizes a side surface of D1.

Original language	English (US)
Pages (from-to)	874-878
Number of pages	5
Journal	Nature Structural Biology
Volume	8
Issue number	10
DOIs	https://doi.org/10.1038/nsb1001-874
State	Published - 2001
Externally published	Yes

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title = "Interaction of coxsackievirus B3 with the full length coxsackievirus-adenovirus receptor",

abstract = "Group B coxsackieviruses (CVB) utilize the coxsackievirus-adenovirus receptor (CAR) to recognize host cells. CAR is a membrane protein with two Ig-like extracellular domains (D1 and D2), a transmembrane domain and a cytoplasmic domain. The three-dimensional structure of coxsackievirus B3 (CVB3) in complex with full length human CAR and also with the D1D2 fragment of CAR were determined to ∼22 {\AA} resolution using cryo-electron microscopy (cryo-EM). Pairs of transmembrane domains of CAR associate with each other in a detergent cloud that mimics a cellular plasma membrane. This is the first view of a virus-receptor interaction at this resolution that includes the transmembrane and cytoplasmic portion of the receptor. CAR binds with the distal end of domain D1 in the canyon of CVB3, similar to how other receptor molecules bind to entero- and rhinoviruses. The previously described interface of CAR with the adenovirus knob protein utilizes a side surface of D1.",

author = "Yongning He and Chipman, \{Paul R.\} and Jason Howitt and Bator, \{Carol M.\} and Whitt, \{Michael A.\} and Baker, \{Timothy S.\} and Kuhn, \{Richard J.\} and Anderson, \{Carl W.\} and Paul Freimuth and Rossmann, \{Michael G.\}",

year = "2001",

doi = "10.1038/nsb1001-874",

language = "English (US)",

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pages = "874--878",

journal = "Nature Structural Biology",

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T1 - Interaction of coxsackievirus B3 with the full length coxsackievirus-adenovirus receptor

AU - He, Yongning

AU - Chipman, Paul R.

AU - Howitt, Jason

AU - Bator, Carol M.

AU - Whitt, Michael A.

AU - Baker, Timothy S.

AU - Kuhn, Richard J.

AU - Anderson, Carl W.

AU - Freimuth, Paul

AU - Rossmann, Michael G.

PY - 2001

Y1 - 2001

N2 - Group B coxsackieviruses (CVB) utilize the coxsackievirus-adenovirus receptor (CAR) to recognize host cells. CAR is a membrane protein with two Ig-like extracellular domains (D1 and D2), a transmembrane domain and a cytoplasmic domain. The three-dimensional structure of coxsackievirus B3 (CVB3) in complex with full length human CAR and also with the D1D2 fragment of CAR were determined to ∼22 Å resolution using cryo-electron microscopy (cryo-EM). Pairs of transmembrane domains of CAR associate with each other in a detergent cloud that mimics a cellular plasma membrane. This is the first view of a virus-receptor interaction at this resolution that includes the transmembrane and cytoplasmic portion of the receptor. CAR binds with the distal end of domain D1 in the canyon of CVB3, similar to how other receptor molecules bind to entero- and rhinoviruses. The previously described interface of CAR with the adenovirus knob protein utilizes a side surface of D1.

AB - Group B coxsackieviruses (CVB) utilize the coxsackievirus-adenovirus receptor (CAR) to recognize host cells. CAR is a membrane protein with two Ig-like extracellular domains (D1 and D2), a transmembrane domain and a cytoplasmic domain. The three-dimensional structure of coxsackievirus B3 (CVB3) in complex with full length human CAR and also with the D1D2 fragment of CAR were determined to ∼22 Å resolution using cryo-electron microscopy (cryo-EM). Pairs of transmembrane domains of CAR associate with each other in a detergent cloud that mimics a cellular plasma membrane. This is the first view of a virus-receptor interaction at this resolution that includes the transmembrane and cytoplasmic portion of the receptor. CAR binds with the distal end of domain D1 in the canyon of CVB3, similar to how other receptor molecules bind to entero- and rhinoviruses. The previously described interface of CAR with the adenovirus knob protein utilizes a side surface of D1.

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JO - Nature Structural Biology

JF - Nature Structural Biology

IS - 10

ER -

Interaction of coxsackievirus B3 with the full length coxsackievirus-adenovirus receptor

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