Abstract
Glycoproteins gB and gH/gL are required for entry of Epstein-Barr virus (EBV) into cells, but the role of each glycoprotein and how they function together to mediate fusion is unclear. Analysis of the functional homology of gB from the closely related primate gammaherpesvirus, rhesus lymphocryptovirus (Rh-LCV), showed that EBV gB could not complement Rh gB due to a species-specific dependence between gB and gL. To map domains of gB required for this interaction, we constructed a panel of EBV/Rh gB chimeric proteins. Analysis showed that insertion of Rh gB from residues 456 to 807 restored fusion function of EBV gB with Rh gH/gL, suggesting this region of gB is important for interaction with gH/gL. Split YFP bimolecular complementation (BiFC) provided evidence of an interaction between EBV gB and gH/gL. Together, our results suggest the importance of a gB-gH/gL interaction in EBV-mediated fusion with B cells requiring the region of EBV gB from 456 to 807.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 26-38 |
| Number of pages | 13 |
| Journal | Virology |
| Volume | 413 |
| Issue number | 1 |
| DOIs | |
| State | Published - Apr 25 2011 |
Funding
We thank Lindsey Hutt-Fletcher for her generous gift of the E1D1 and CL55 antibody cell line. Gary Cohen and Roz Eisenberg for kindly proving the constructs used for BiFC and Fred Wang for providing the DNA used fort the construction of the Rhesus glycoprotein expression vectors. Finally, we thank the members of the Longnecker and Jardetzky laboratories for help and support. This research was supported by AI076183 (R.L. and T.J.) and AI067048 (R.L.) from National Institute of Allergy and Infectious Diseases and CA117794 (R.L. and T.J.) from the National Cancer Institute . A.P. is supported by a pre-doctoral training award from the American Heart Association .
Keywords
- Epstein-Barr virus
- Fusion
- Glycoprotein gB
- Glycoprotein gH
- Glycoprotein gL
- Lymphocryptovirus
- Rhesus
ASJC Scopus subject areas
- Virology