A B-lymphocyte binding peptide from BNRF1 induced antibodies inhibiting EBV-invasion of B-lymphocytes
Epstein–Barr virus (EBV) infects human target cells mainly through gp350/220-CD21 and gp42-MHCII interactions; however, it has been shown that these interactions are dispensable for EBV-invasion of susceptible cells, suggesting that other viral proteins are involved in this process. It is probable t...
- Autores:
- Tipo de recurso:
- Fecha de publicación:
- 2005
- Institución:
- Universidad del Rosario
- Repositorio:
- Repositorio EdocUR - U. Rosario
- Idioma:
- eng
- OAI Identifier:
- oai:repository.urosario.edu.co:10336/25880
- Acceso en línea:
- https://doi.org/10.1016/j.biochi.2005.04.009
https://repository.urosario.edu.co/handle/10336/25880
- Palabra clave:
- EBV
p140
HABP
B-lymphocyte
- Rights
- License
- Restringido (Acceso a grupos específicos)
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EDOCUR2 |
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Repositorio EdocUR - U. Rosario |
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2545c992-99b1-4106-8dc9-0a8d111b2438-1dd3af730-1a89-42fc-a5de-64665dc12a41-16cdae981-0158-4265-8703-408b9e3d3cd8-164e2fd99-86b7-4e34-9d38-c4ae6270a272-16fc431a4-2889-4e78-ba01-10c2807c6557-179653065-110ecd4f9-843f-4ef2-bec0-7d39d3381a13-12020-08-06T16:20:07Z2020-08-06T16:20:07Z2005-11Epstein–Barr virus (EBV) infects human target cells mainly through gp350/220-CD21 and gp42-MHCII interactions; however, it has been shown that these interactions are dispensable for EBV-invasion of susceptible cells, suggesting that other viral proteins are involved in this process. It is probable that tegument BNRF1/p140 protein is involved in EBV-invasion of target cells, since anti-p140 antibodies inhibit EBV-infection of B-lymphocytes and there is evidence that part of the protein is located on virus surface. Sixty-six peptides, covering the entire BNRF1/p140 sequence, were synthesised and tested in lymphoblastoid cell line binding assays. Peptides 11465 and 11521 bound with high affinity to Raji, Ramos and P3HR-1 cells but not to erythrocytes, showing cell-binding behaviour similar to EBV. These two peptides induced antibodies recognising live EBV-infected cells. Interestingly, peptide-11521 (YVLQNAHQIACHFHSNGTDA) or antibodies induced by this peptide inhibited EBV-binding to B-lymphocytes, suggesting that this p140-region could be involved in EBV and B-lymphocyte interaction.application/pdfhttps://doi.org/10.1016/j.biochi.2005.04.009ISSN: 0300-9084EISSN: 6183-1638https://repository.urosario.edu.co/handle/10336/25880engElsevier992No. 11985BiochimieVol. 87Biochimie, ISSN: 0300-9084;EISSN: 6183-1638, Vol. 87 No.11 (2005); pp.985-992https://www.sciencedirect.com/science/article/abs/pii/S0300908405001057?via%3DihubRestringido (Acceso a grupos específicos)http://purl.org/coar/access_right/c_16ecBiochimieinstname:Universidad del Rosarioreponame:Repositorio Institucional EdocUREBVp140HABPB-lymphocyteA B-lymphocyte binding peptide from BNRF1 induced antibodies inhibiting EBV-invasion of B-lymphocytesUn péptido de unión a linfocitos B de anticuerpos inducidos por BNRF1 que inhiben la invasión de linfocitos B por el EBVarticleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501López, RamsésUrquiza, MauricioPatino, HelenaSuárez, JorgeReyes, ClaudiaPatarroyo, Manuel A.Patarroyo, Manuel E.10336/25880oai:repository.urosario.edu.co:10336/258802022-05-02 07:37:15.222147https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co |
dc.title.spa.fl_str_mv |
A B-lymphocyte binding peptide from BNRF1 induced antibodies inhibiting EBV-invasion of B-lymphocytes |
dc.title.TranslatedTitle.spa.fl_str_mv |
Un péptido de unión a linfocitos B de anticuerpos inducidos por BNRF1 que inhiben la invasión de linfocitos B por el EBV |
title |
A B-lymphocyte binding peptide from BNRF1 induced antibodies inhibiting EBV-invasion of B-lymphocytes |
spellingShingle |
A B-lymphocyte binding peptide from BNRF1 induced antibodies inhibiting EBV-invasion of B-lymphocytes EBV p140 HABP B-lymphocyte |
title_short |
A B-lymphocyte binding peptide from BNRF1 induced antibodies inhibiting EBV-invasion of B-lymphocytes |
title_full |
A B-lymphocyte binding peptide from BNRF1 induced antibodies inhibiting EBV-invasion of B-lymphocytes |
title_fullStr |
A B-lymphocyte binding peptide from BNRF1 induced antibodies inhibiting EBV-invasion of B-lymphocytes |
title_full_unstemmed |
A B-lymphocyte binding peptide from BNRF1 induced antibodies inhibiting EBV-invasion of B-lymphocytes |
title_sort |
A B-lymphocyte binding peptide from BNRF1 induced antibodies inhibiting EBV-invasion of B-lymphocytes |
dc.subject.keyword.spa.fl_str_mv |
EBV p140 HABP B-lymphocyte |
topic |
EBV p140 HABP B-lymphocyte |
description |
Epstein–Barr virus (EBV) infects human target cells mainly through gp350/220-CD21 and gp42-MHCII interactions; however, it has been shown that these interactions are dispensable for EBV-invasion of susceptible cells, suggesting that other viral proteins are involved in this process. It is probable that tegument BNRF1/p140 protein is involved in EBV-invasion of target cells, since anti-p140 antibodies inhibit EBV-infection of B-lymphocytes and there is evidence that part of the protein is located on virus surface. Sixty-six peptides, covering the entire BNRF1/p140 sequence, were synthesised and tested in lymphoblastoid cell line binding assays. Peptides 11465 and 11521 bound with high affinity to Raji, Ramos and P3HR-1 cells but not to erythrocytes, showing cell-binding behaviour similar to EBV. These two peptides induced antibodies recognising live EBV-infected cells. Interestingly, peptide-11521 (YVLQNAHQIACHFHSNGTDA) or antibodies induced by this peptide inhibited EBV-binding to B-lymphocytes, suggesting that this p140-region could be involved in EBV and B-lymphocyte interaction. |
publishDate |
2005 |
dc.date.created.spa.fl_str_mv |
2005-11 |
dc.date.accessioned.none.fl_str_mv |
2020-08-06T16:20:07Z |
dc.date.available.none.fl_str_mv |
2020-08-06T16:20:07Z |
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.biochi.2005.04.009 |
dc.identifier.issn.none.fl_str_mv |
ISSN: 0300-9084 EISSN: 6183-1638 |
dc.identifier.uri.none.fl_str_mv |
https://repository.urosario.edu.co/handle/10336/25880 |
url |
https://doi.org/10.1016/j.biochi.2005.04.009 https://repository.urosario.edu.co/handle/10336/25880 |
identifier_str_mv |
ISSN: 0300-9084 EISSN: 6183-1638 |
dc.language.iso.spa.fl_str_mv |
eng |
language |
eng |
dc.relation.citationEndPage.none.fl_str_mv |
992 |
dc.relation.citationIssue.none.fl_str_mv |
No. 11 |
dc.relation.citationStartPage.none.fl_str_mv |
985 |
dc.relation.citationTitle.none.fl_str_mv |
Biochimie |
dc.relation.citationVolume.none.fl_str_mv |
Vol. 87 |
dc.relation.ispartof.spa.fl_str_mv |
Biochimie, ISSN: 0300-9084;EISSN: 6183-1638, Vol. 87 No.11 (2005); pp.985-992 |
dc.relation.uri.spa.fl_str_mv |
https://www.sciencedirect.com/science/article/abs/pii/S0300908405001057?via%3Dihub |
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 |
Biochimie |
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_ |
1828160525199998976 |