Previous Article | Next Article 
Journal of Virology, October 2005, p. 12408-12415, Vol. 79, No. 19
0022-538X/05/$08.00+0 doi:10.1128/JVI.79.19.12408-12415.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
The Amino Terminus of Epstein-Barr Virus Glycoprotein gH Is Important for Fusion with Epithelial and B Cells
Jasmina Omerovi
,
Lori Lev, and
Richard Longnecker*
Department of Microbiology and Immunology, The Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60611
Received 30 April 2005/
Accepted 8 July 2005
Epstein-Barr virus (EBV) infects B lymphocytes and epithelial cells. While the glycoproteins required for entry into these two cell types differ, the gH/gL glycoprotein complex is essential for entry into both epithelial and B cells. Analysis of gH protein sequences from three gammaherpesviruses (EBV, marmoset, and rhesus) revealed a potential coiled-coil domain in the N terminus. Four leucines located in this region in EBV gH were replaced by alanines by site-directed mutagenesis and analyzed for cell-cell membrane fusion with B cells and epithelial cells. Reduction in fusion activity was observed for mutants containing L65A and/or L69A mutations, while substitutions in L55 and L74 enhanced the fusion activity of the mutant gH/gL complexes with both cell types. All of the mutants displayed levels of cell surface expression similar to those of wild-type gH and interacted with gL and gp42. The observation that a conservative mutation of leucine to alanine in the N terminus of EBV gH results in fusion-defective mutant gH/gL complexes is striking and points to an important role for this region in EBV-mediated membrane fusion with B lymphocytes and epithelial cells.
* Corresponding author. Mailing address: Department of Microbiology and Immunology, The Feinberg School of Medicine, Northwestern University, Ward 6-231, 303 E. Chicago Ave., Chicago, IL 60611. Phone: (312) 503-0467. Fax: (312) 503-1339. E-mail:
r-longnecker{at}northwestern.edu.
Journal of Virology, October 2005, p. 12408-12415, Vol. 79, No. 19
0022-538X/05/$08.00+0 doi:10.1128/JVI.79.19.12408-12415.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
This article has been cited by other articles:
-
Plate, A. E., Smajlovic, J., Jardetzky, T. S., Longnecker, R.
(2009). Functional Analysis of Glycoprotein L (gL) from Rhesus Lymphocryptovirus in Epstein-Barr Virus-Mediated Cell Fusion Indicates a Direct Role of gL in gB-Induced Membrane Fusion. J. Virol.
83: 7678-7689
[Abstract]
[Full Text]
-
Sorem, J., Longnecker, R.
(2009). Cleavage of Epstein-Barr virus glycoprotein B is required for full function in cell-cell fusion with both epithelial and B cells. J. Gen. Virol.
90: 591-595
[Abstract]
[Full Text]
-
Reimer, J. J., Backovic, M., Deshpande, C. G., Jardetzky, T., Longnecker, R.
(2009). Analysis of Epstein-Barr Virus Glycoprotein B Functional Domains via Linker Insertion Mutagenesis. J. Virol.
83: 734-747
[Abstract]
[Full Text]
-
de Oliveira, A. P., Glauser, D. L., Laimbacher, A. S., Strasser, R., Schraner, E. M., Wild, P., Ziegler, U., Breakefield, X. O., Ackermann, M., Fraefel, C.
(2008). Live Visualization of Herpes Simplex Virus Type 1 Compartment Dynamics. J. Virol.
82: 4974-4990
[Abstract]
[Full Text]
-
Backovic, M., Jardetzky, T. S., Longnecker, R.
(2007). Hydrophobic Residues That Form Putative Fusion Loops of Epstein-Barr Virus Glycoprotein B Are Critical for Fusion Activity. J. Virol.
81: 9596-9600
[Abstract]
[Full Text]
-
Kirschner, A. N., Lowrey, A. S., Longnecker, R., Jardetzky, T. S.
(2007). Binding-Site Interactions between Epstein-Barr Virus Fusion Proteins gp42 and gH/gL Reveal a Peptide That Inhibits both Epithelial and B-Cell Membrane Fusion. J. Virol.
81: 9216-9229
[Abstract]
[Full Text]
-
Wu, L., Hutt-Fletcher, L. M.
(2007). Compatibility of the gH homologues of Epstein-Barr virus and related lymphocryptoviruses. J. Gen. Virol.
88: 2129-2136
[Abstract]
[Full Text]
-
Hutt-Fletcher, L. M.
(2007). Epstein-Barr Virus Entry. J. Virol.
81: 7825-7832
[Full Text]
-
Kirschner, A. N., Omerovic, J., Popov, B., Longnecker, R., Jardetzky, T. S.
(2006). Soluble Epstein-Barr Virus Glycoproteins gH, gL, and gp42 Form a 1:1:1 Stable Complex That Acts Like Soluble gp42 in B-Cell Fusion but Not in Epithelial Cell Fusion. J. Virol.
80: 9444-9454
[Abstract]
[Full Text]
-
Gianni, T., Fato, R., Bergamini, C., Lenaz, G., Campadelli-Fiume, G.
(2006). Hydrophobic {alpha}-Helices 1 and 2 of Herpes Simplex Virus gH Interact with Lipids, and Their Mimetic Peptides Enhance Virus Infection and Fusion.. J. Virol.
80: 8190-8198
[Abstract]
[Full Text]
-
Gianni, T., Piccoli, A., Bertucci, C., Campadelli-Fiume, G.
(2006). Heptad Repeat 2 in Herpes Simplex Virus 1 gH Interacts with Heptad Repeat 1 and Is Critical for Virus Entry and Fusion. J. Virol.
80: 2216-2224
[Abstract]
[Full Text]