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Journal of Virology, September 1999, p. 7830-7834, Vol. 73, No. 9
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Three-Dimensional Structure of Herpes Simplex Virus Type 1 Glycoprotein D at 2.4-Nanometer Resolution

Andrew Pilling,1,2 Mark F. Rosenberg,3 Sharon H. Willis,4 Joachim Jäger,2 Gary H. Cohen,4 Roselyn J. Eisenberg,5 David M. Meredith,1 and Andreas Holzenburg2,6,*

Schools of Biochemistry and Molecular Biology2 and Biology,6 University of Leeds, Leeds LS2 9JT, Centre for Molecular Medicine, St. James's University Hospital, University of Leeds, Leeds LS9 7TF,1 and Department of Biomolecular Sciences, UMIST, Manchester M60 1QD,3 United Kingdom, and School of Dental Medicine, Center for Oral Health Research,4 and School of Veterinary Medicine,5 University of Pennsylvania, Philadelphia, Pennsylvania 19104

Received 15 March 1999/Accepted 27 May 1999

Herpes simplex virus type 1 glycoprotein D (gD) is essential for virus infectivity and is responsible for binding to cellular membrane proteins and subsequently promoting fusion between the virus envelope and the cell. No structural data are available for gD or for any other herpesvirus envelope protein. Here we present a three-dimensional model for the baculovirus-expressed truncated protein gD1(306t) based on electron microscopic data. We demonstrate that gD1(306t) appears as a homotetramer containing a pronounced pocket in the center of the molecule. Monoclonal antibody binding demonstrates that the molecule is oriented such that the pocket protrudes away from the virus envelope.

* Corresponding author. Mailing address: School of Biochemistry and Molecular Biology and School of Biology, The University of Leeds, Leeds LS2 9JT, United Kingdom. Phone: 44-113-233 2590. Fax: 44-113-233 3167. E-mail: holzen{at}bmb.leeds.ac.uk.

Journal of Virology, September 1999, p. 7830-7834, Vol. 73, No. 9
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.




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Copyright © 1999 by the American Society for Microbiology. All rights reserved.