Interaction of coxsackievirus B3 with the full length coxsackievirus-adenovirus receptor.
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 approximately 22 A 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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Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, USA.
Chipman
P R
PR
Howitt
J
J
Bator
C M
CM
Whitt
M A
MA
Baker
T S
TS
Kuhn
R J
RJ
Anderson
C W
CW
Freimuth
P
P
Rossmann
M G
MG
D000256:Adenoviridae / Q000737:chemistry / Q000378:metabolism*; D029822:Enterovirus B, Human / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D008854:Microscopy, Electron / Q000379:methods; D008958:Models, Molecular; D011991:Receptors, Virus / Q000737:chemistry / Q000378:metabolism*; D010948:Viral Plaque Assay
D011991:Receptors, Virus