TY - JOUR
T1 - Herpes simplex virus glycoprotein D bound to the human receptor HveA
AU - Carfí, Andrea
AU - Willis, Sharon H.
AU - Whitbeck, J. Charles
AU - Krummenacher, Claude
AU - Cohen, Gary H.
AU - Eisenberg, Roselyn J.
AU - Wiley, Don C.
N1 - Funding Information:
The research was supported by the National Institutes of Health (AI18289, NS36731, and NS30606 to R.J.E. and G.H.C.) and the Howard Hughes Medical Institute (HHMI). A.C. was supported by a fellowship from the Irvington Institute for Immunological Research. D.C.W. is an investigator of the HHMI. We thank Haiyun Gong and Huan Lou for excellent technical assistance; Micah Luftig, Dr. Bing Chen, and Dr. Ya Ha for discussions; the staff at APS at Argonne National Laboratory beamlines BIOCARS 14-BM-C and 14-BM-D, at CHESS beam line A1, and at Brookhaven National Laboratory beam line X25 for help with data collection; and members of the Harrison/Wiley and Eisenberg/Cohen groups for assistance.
PY - 2001
Y1 - 2001
N2 - Herpes simplex virus (HSV) infection requires binding of the viral envelope glycoprotein D (gD) to cell surface receptors. We report the X-ray structures of a soluble, truncated ectodomain of gD both alone and in complex with the ectodomain of its cellular receptor HveA. Two bound anions suggest possible binding sites for another gD receptor, a 3-O-sulfonated heparan sulfate. Unexpectedly, the structures reveal a V-like immunoglobulin (Ig) fold at the core of gD that is closely related to cellular adhesion molecules and flanked by large N- and C-terminal extensions. The receptor binding segment of gD, an N-terminal hairpin, appears conformationally flexible, suggesting that a conformational change accompanying binding might be part of the viral entry mechanism.
AB - Herpes simplex virus (HSV) infection requires binding of the viral envelope glycoprotein D (gD) to cell surface receptors. We report the X-ray structures of a soluble, truncated ectodomain of gD both alone and in complex with the ectodomain of its cellular receptor HveA. Two bound anions suggest possible binding sites for another gD receptor, a 3-O-sulfonated heparan sulfate. Unexpectedly, the structures reveal a V-like immunoglobulin (Ig) fold at the core of gD that is closely related to cellular adhesion molecules and flanked by large N- and C-terminal extensions. The receptor binding segment of gD, an N-terminal hairpin, appears conformationally flexible, suggesting that a conformational change accompanying binding might be part of the viral entry mechanism.
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U2 - 10.1016/S1097-2765(01)00298-2
DO - 10.1016/S1097-2765(01)00298-2
M3 - Article
C2 - 11511370
AN - SCOPUS:0034892857
SN - 1097-2765
VL - 8
SP - 169
EP - 179
JO - Molecular Cell
JF - Molecular Cell
IS - 1
ER -