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.
journal_name
Virologyjournal_title
Virologyauthors
Plate AE,Reimer JJ,Jardetzky TS,Longnecker Rdoi
10.1016/j.virol.2010.12.006subject
Has Abstractpub_date
2011-04-25 00:00:00pages
26-38issue
1eissn
0042-6822issn
1096-0341pii
S0042-6822(10)00750-6journal_volume
413pub_type
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