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

Author:

Pilling Andrew12,Rosenberg Mark F.3,Willis Sharon H.4,Jäger Joachim1,Cohen Gary H.4,Eisenberg Roselyn J.5,Meredith David M.2,Holzenburg Andreas16

Affiliation:

1. Schools of Biochemistry and Molecular Biology2 and

2. Centre for Molecular Medicine, St. James’s University Hospital, University of Leeds, Leeds LS9 7TF,1 and

3. Department of Biomolecular Sciences, UMIST, Manchester M60 1QD,3 United Kingdom, and

4. School of Dental Medicine, Center for Oral Health Research,4 and

5. School of Veterinary Medicine,5 University of Pennsylvania, Philadelphia, Pennsylvania 19104

6. Biology,6University of Leeds, Leeds LS2 9JT,

Abstract

ABSTRACT 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.

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

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