Identifying gp85- regions involved in Epstein- Barr virus binding to Blymphocytes.
Epstein–Barr virus lacking glycoprotein gp85 cannot infect B-cells and epithelial cells. The gp85 belongs to the molecular complex required for virus invasion of B-lymphocyte or epithelial cells. Moreover, there is evidence that gp85 is necessary for virus attachment to epithelial cells. Thirty-six...
- Autores:
- Tipo de recurso:
- Fecha de publicación:
- 2004
- Institución:
- Universidad del Rosario
- Repositorio:
- Repositorio EdocUR - U. Rosario
- Idioma:
- eng
- OAI Identifier:
- oai:repository.urosario.edu.co:10336/27839
- Acceso en línea:
- https://doi.org/10.1016/j.bbrc.2004.04.177
https://repository.urosario.edu.co/handle/10336/27839
- Palabra clave:
- EBV
gp85
Raji-cell binding peptides
HABPs
- Rights
- License
- Restringido (Acceso a grupos específicos)
Summary: | Epstein–Barr virus lacking glycoprotein gp85 cannot infect B-cells and epithelial cells. The gp85 belongs to the molecular complex required for virus invasion of B-lymphocyte or epithelial cells. Moreover, there is evidence that gp85 is necessary for virus attachment to epithelial cells. Thirty-six peptides from the entire gp85-sequence were tested in epithelial and lymphoblastoid cell line binding assays to identify gp85-regions involved in virus–cell interaction. Five of these peptides presented high binding activity to Raji, Ramos, P3HR-1, and HeLa cells, but not to erythrocytes; Raji-cell affinity constants were between 80 and 140 nM. Of these five peptides, 11435 (181TYKRVTEKGDEHVLSLVFGK200), 11436 (201TKDLPDLRGPFSYPSLTSAQ220), and 11438 (241YFVPNLKDMFSRAVTMTAAS260) bound to a 65 kDa protein on Raji-cell surface. These peptides and antibodies induced by them (recognising live EBV-infected cells) inhibited Epstein–Barr virus interaction with cord blood lymphocytes. It is thus probable that gp85-regions defined by peptides 11435, 11436, and 11438 are involved in EBV invasion of B-lymphocytes. |
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