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Journal of Virology, August 2009, p. 7678-7689, Vol. 83, No. 15
0022-538X/09/$08.00+0     doi:10.1128/JVI.00457-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

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{triangledown}

Aileen E. Plate,1 Jasmina Smajlovic,1,# Theodore S. Jardetzky,2 and Richard Longnecker1*

Department of Microbiology and Immunology, The Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60611,1 Department of Structural Biology, Stanford University School of Medicine, 371 Serra Mall, Stanford, California 943052

Received 4 March 2009/ Accepted 14 May 2009

Glycoprotein L (gL), which complexes with gH, is a conserved herpesvirus protein that is essential for Epstein-Barr virus (EBV) entry into host cells. The gH/gL complex has a conserved role in entry among herpesviruses, yet the mechanism is not clear. To gain a better understanding of the role of gL in EBV-mediated fusion, chimeric proteins were made using rhesus lymphocryptovirus (Rh-LCV) gL (Rh gL), which shares a high sequence homology with EBV gL but does not complement EBV gL in mediating fusion with B cells. A reduction in fusion activity was observed with chimeric gL proteins that contained the amino terminus of Rh gL, although they retained their ability to process and transport gH/gL to the cell surface. Amino acids not conserved within this region in EBV gL when compared to Rh gL were further analyzed, with the results mapping residues 54 and 94 as being functionally important for EBV-mediated fusion. All chimeras and mutants displayed levels of cell surface expression similar to that of wild-type gL and interacted with gH and gp42. Our data also suggest that the role of gL involves the activation or recruitment of gB with the gH/gL complex, as we found that reduced fusion of Rh gL, EBV/Rh-LCV chimeras, and gL point mutants could be restored by replacing EBV gB with Rh gB. These observations demonstrate a distinction between the role of gL in the processing and trafficking of gH to the cell surface and a posttrafficking role in cell-cell fusion.

* Corresponding author. Mailing address: Northwestern University, Department of Microbiology and Immunology, 303 E. Chicago Avenue, Chicago, IL 60611. Phone: (312) 503-0467. Fax: (312) 503-1339. E-mail: r-longnecker{at}northwestern.edu

{triangledown} Published ahead of print on 20 May 2009.

# Present address: Department of Molecular Microbiology, University Clinical Center Tuzla, Tuzla, Bosnia and Herzegovina.

Journal of Virology, August 2009, p. 7678-7689, Vol. 83, No. 15
0022-538X/09/$08.00+0     doi:10.1128/JVI.00457-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Fan, Q., Lin, E., Spear, P. G. (2009). Insertional Mutations in Herpes Simplex Virus Type 1 gL Identify Functional Domains for Association with gH and for Membrane Fusion. J. Virol. 83: 11607-11615 [Abstract] [Full Text]  


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