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Journal of Virology, June 2004, p. 5946-5956, Vol. 78, No. 11
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.11.5946-5956.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Mutational Analyses of Epstein-Barr Virus Glycoprotein 42 Reveal Functional Domains Not Involved in Receptor Binding but Required for Membrane Fusion

Amanda L. Silva,1 Jasmina Omerovi,1 Theodore S. Jardetzky,2 and Richard Longnecker1*

Department of Microbiology and Immunology, Northwestern University Medical School, Chicago, Illinois 60611,1 Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 602082

Received 30 October 2003/ Accepted 15 January 2004

Epstein-Barr virus (EBV) is a human gammaherpesvirus associated with malignancies of both epithelial and lymphoid origin. Efficient infection of the latent host reservoir B lymphocytes involves the binding of glycoproteins gp350/220 for initial attachment, followed by the concerted action of gH, gL, gB, and gp42 for membrane fusion. The type II membrane protein gp42 is required for infection of B cells and assembles into a complex with gH and gL. The cellular host receptor for gp42, class II human leukocyte antigen (HLA), has been structurally verified by crystallization analyses of gp42 bound to HLA-DR1. Interestingly, the crystal structure revealed a hydrophobic pocket consisting of many aromatic and aliphatic residues from the predicted C-type lectin domain of gp42 that in other members of the C-type lectin family binds major histocompatibility complex class I or other diverse ligands. Although the hydrophobic pocket does not bind HLA class II, mutational analyses presented here indicate that this domain is essential for EBV-induced membrane fusion. In addition, mutational analysis of the region of gp42 contacting HLA class II in the gp42-HLA-DR1 cocrystal confirms that this region interacts with HLA class II and that this interaction is also important for EBV-induced membrane fusion.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, Northwestern University Medical School, Ward 6-231, Chicago, IL 60611. Phone: (312) 503-0467. Fax: (312) 503-1339. E-mail: r-longnecker{at}northwestern.edu.

Journal of Virology, June 2004, p. 5946-5956, Vol. 78, No. 11
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.11.5946-5956.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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