Functional homology of gHs and gLs from EBV-related γ-herpesviruses for EBV-induced membrane fusion
| Autor: | Richard Longnecker, Jasmina Omerović |
|---|---|
| Jazyk: | angličtina |
| Předmět: |
Herpesvirus 4
Human CHO Cells medicine.disease_cause Glycoprotein gp42 Membrane Fusion Article Virus Lymphocryptovirus Epstein–Barr virus Viral Proteins 03 medical and health sciences Cricetulus Glycoprotein gL Cricetinae Virology medicine Animals HHV8 Fusion Glycoproteins 030304 developmental biology Glycoprotein gH chemistry.chemical_classification B-Lymphocytes 0303 health sciences Cell fusion biology Chinese hamster ovary cell 030302 biochemistry & molecular biology Epithelial Cells biology.organism_classification Herpesvirus glycoprotein B 3. Good health Cross-virus complementation chemistry Herpesvirus 8 Human Glycoprotein Oncovirus |
| Zdroj: | Virology. (1):157-165 |
| ISSN: | 0042-6822 |
| DOI: | 10.1016/j.virol.2007.03.054 |
| Popis: | Epstein-Barr virus (EBV) is a human gamma-herpesvirus that primarily infects B lymphocytes and epithelial cells. Entry of EBV into B cells requires the viral glycoproteins gp42, gH/gL and gB, while gp42 is not necessary for infection of epithelial cells. In EBV, gH and gL form two distinct complexes, a bipartite complex that contains only gH and gL, used for infection of epithelial cells, and a tripartite complex that additionally includes gp42, used for infection of B cells. The gH/gL complex is conserved within the herpesvirus family, but its exact role in entry and mechanism of fusion is not yet known. To understand more about the functionality of EBVgH/gL, we investigated the functional homology of gHs and gLs from human herpesvirus 8 (HHV8) and two primate (rhesus and marmoset) gamma-herpesviruses in EBV-mediated virus-free cell fusion assay. Overall, gHs and gLs from the more homologous primate herpesviruses were better at complementing EBV gH and gL in fusion than HHV8 gH and gL. Interestingly, marmoset gH was able to complement fusion with epithelial cells, but not B cells. Further investigation of this led to the discovery that EBVgH is the binding partner of gp42 in the tripartite complex and the absence of fusion with B cells in the presence of marmoset gH/gL is due to its inability to bind gp42. |
| Databáze: | OpenAIRE |
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