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)
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EDOCUR2 |
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Repositorio EdocUR - U. Rosario |
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dd3af730-1a89-42fc-a5de-64665dc12a41-1c4dd6f1e-a512-4c2f-87d2-d8ff29ce6096-1e24a8b75-8725-433a-8f7d-b1de864249ab-1b6e32984-5d22-45d8-920f-88382058bfc1-1f80963bb-2585-42c7-9d23-4b3face7eb29-1b8902bd8-16f9-4e10-84ce-847819e12c56-179653065-1606513c1-aaa4-4683-beee-4c4213f14cc9-110ecd4f9-843f-4ef2-bec0-7d39d3381a13-12020-08-19T14:44:10Z2020-08-19T14:44:10Z2004Epstein–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.application/pdfhttps://doi.org/10.1016/j.bbrc.2004.04.177ISSN: 0006-291XEISSN: 1090-2104https://repository.urosario.edu.co/handle/10336/27839engElsevier229No. 1221Biochemical and Biophysical Research CommunicationsVol. 319Biochemical and Biophysical Research Communications, ISSN: 0006-291X ; EISSN: 1090-2104, Vol.319, No.1 (18 June 2004); pp. 221-229https://www.sciencedirect.com/science/article/abs/pii/S0006291X04009453Restringido (Acceso a grupos específicos)http://purl.org/coar/access_right/c_16ecBiochemical and Biophysical Research Communicationsinstname:Universidad del Rosarioreponame:Repositorio Institucional EdocUREBVgp85Raji-cell binding peptidesHABPsIdentifying gp85- regions involved in Epstein- Barr virus binding to Blymphocytes.Identificación de las regiones gp85- implicadas en la unión del virus de Epstein-Barr a los linfocitos B.articleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Urquiza, MauricioSuarez, JorgeLopez, RamsesVega, ErikaPatiño, HelenaGarcia, JavierPatarroyo, Manuel A.Guzman, FannyPatarroyo, Manuel E.10336/27839oai:repository.urosario.edu.co:10336/278392022-05-02 07:37:21.936144https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co |
dc.title.spa.fl_str_mv |
Identifying gp85- regions involved in Epstein- Barr virus binding to Blymphocytes. |
dc.title.TranslatedTitle.spa.fl_str_mv |
Identificación de las regiones gp85- implicadas en la unión del virus de Epstein-Barr a los linfocitos B. |
title |
Identifying gp85- regions involved in Epstein- Barr virus binding to Blymphocytes. |
spellingShingle |
Identifying gp85- regions involved in Epstein- Barr virus binding to Blymphocytes. EBV gp85 Raji-cell binding peptides HABPs |
title_short |
Identifying gp85- regions involved in Epstein- Barr virus binding to Blymphocytes. |
title_full |
Identifying gp85- regions involved in Epstein- Barr virus binding to Blymphocytes. |
title_fullStr |
Identifying gp85- regions involved in Epstein- Barr virus binding to Blymphocytes. |
title_full_unstemmed |
Identifying gp85- regions involved in Epstein- Barr virus binding to Blymphocytes. |
title_sort |
Identifying gp85- regions involved in Epstein- Barr virus binding to Blymphocytes. |
dc.subject.keyword.spa.fl_str_mv |
EBV gp85 Raji-cell binding peptides HABPs |
topic |
EBV gp85 Raji-cell binding peptides HABPs |
description |
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. |
publishDate |
2004 |
dc.date.created.spa.fl_str_mv |
2004 |
dc.date.accessioned.none.fl_str_mv |
2020-08-19T14:44:10Z |
dc.date.available.none.fl_str_mv |
2020-08-19T14:44:10Z |
dc.type.eng.fl_str_mv |
article |
dc.type.coarversion.fl_str_mv |
http://purl.org/coar/version/c_970fb48d4fbd8a85 |
dc.type.coar.fl_str_mv |
http://purl.org/coar/resource_type/c_6501 |
dc.type.spa.spa.fl_str_mv |
Artículo |
dc.identifier.doi.none.fl_str_mv |
https://doi.org/10.1016/j.bbrc.2004.04.177 |
dc.identifier.issn.none.fl_str_mv |
ISSN: 0006-291X EISSN: 1090-2104 |
dc.identifier.uri.none.fl_str_mv |
https://repository.urosario.edu.co/handle/10336/27839 |
url |
https://doi.org/10.1016/j.bbrc.2004.04.177 https://repository.urosario.edu.co/handle/10336/27839 |
identifier_str_mv |
ISSN: 0006-291X EISSN: 1090-2104 |
dc.language.iso.spa.fl_str_mv |
eng |
language |
eng |
dc.relation.citationEndPage.none.fl_str_mv |
229 |
dc.relation.citationIssue.none.fl_str_mv |
No. 1 |
dc.relation.citationStartPage.none.fl_str_mv |
221 |
dc.relation.citationTitle.none.fl_str_mv |
Biochemical and Biophysical Research Communications |
dc.relation.citationVolume.none.fl_str_mv |
Vol. 319 |
dc.relation.ispartof.spa.fl_str_mv |
Biochemical and Biophysical Research Communications, ISSN: 0006-291X ; EISSN: 1090-2104, Vol.319, No.1 (18 June 2004); pp. 221-229 |
dc.relation.uri.spa.fl_str_mv |
https://www.sciencedirect.com/science/article/abs/pii/S0006291X04009453 |
dc.rights.coar.fl_str_mv |
http://purl.org/coar/access_right/c_16ec |
dc.rights.acceso.spa.fl_str_mv |
Restringido (Acceso a grupos específicos) |
rights_invalid_str_mv |
Restringido (Acceso a grupos específicos) http://purl.org/coar/access_right/c_16ec |
dc.format.mimetype.none.fl_str_mv |
application/pdf |
dc.publisher.spa.fl_str_mv |
Elsevier |
dc.source.spa.fl_str_mv |
Biochemical and Biophysical Research Communications |
institution |
Universidad del Rosario |
dc.source.instname.none.fl_str_mv |
instname:Universidad del Rosario |
dc.source.reponame.none.fl_str_mv |
reponame:Repositorio Institucional EdocUR |
repository.name.fl_str_mv |
Repositorio institucional EdocUR |
repository.mail.fl_str_mv |
edocur@urosario.edu.co |
_version_ |
1814167501879115776 |