Identifying plasmodium falciparum EBA-175 homologue sequences that specifically bind to human erythrocytes
Erythrocyte binding antigen-160 (EBA-160) protein is a Plasmodium falciparum antigen homologue from the erythrocyte binding protein family (EBP). It has been shown that the EBP family plays a role in parasite binding to the erythrocyte surface. The EBA-160 sequence has been chemically synthesised in...
- 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:10336/25894
- Acceso en línea:
- https://doi.org/10.1016/j.bbrc.2004.07.034
https://repository.urosario.edu.co/handle/10336/25894
- Palabra clave:
- Erythrocyte binding antigen-160
High activity binding peptides
Plasmodium falciparum
- Rights
- License
- Restringido (Acceso a grupos específicos)
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ea0f406d-cf63-4f20-9cd3-eee998867f9f-10ad382b4-d6b1-4878-a4a1-bd78fc45e107-15e82e691-ba88-4d28-b934-b924d1350834-1ef6547b6-3130-435a-8a09-7ca050cd7b64-191225589-1f2d05f42-2948-4c51-8389-8c3817c2d0f1-1a650efd0-af5f-4ce9-9620-e1cad93a9173-1fa33b517-50cf-4bb5-a980-3773caf84cd8-126af4032-55ab-47ab-acea-77c7596a346d-1546c8cde-3bc3-46e4-afd4-3533e1aba09d-19e3ba9df-fe89-48fe-9521-cc8f452d56f5-1518488266002020-08-06T16:20:09Z2020-08-06T16:20:09Z2004-09-03Erythrocyte binding antigen-160 (EBA-160) protein is a Plasmodium falciparum antigen homologue from the erythrocyte binding protein family (EBP). It has been shown that the EBP family plays a role in parasite binding to the erythrocyte surface. The EBA-160 sequence has been chemically synthesised in seventy 20-mer sequential peptides covering the entire 3D7 protein strain, each of which was tested in erythrocyte binding assays to identify possible EBA-160 functional regions. Five EBA-160 high activity binding peptides (HABPs) specifically binding to erythrocytes with high affinity were identified. Dissociation constants lay between 200 and 460 nM and Hill coefficients between 1.5 and 2.3. Erythrocyte membrane protein binding peptide cross-linking assays using SDS–PAGE showed that these peptides bound specifically to 12, 28, and 44 kDa erythrocyte membrane proteins. The nature of these receptor sites was studied in peptide binding assays using enzyme-treated erythrocytes. HABPs were able to block merozoite in vitro invasion of erythrocytes. HABPs’ potential as anti-malarial vaccine candidates is also discussed.application/pdfhttps://doi.org/10.1016/j.bbrc.2004.07.034ISSN: 0006-291XEISSN: 1090-2104https://repository.urosario.edu.co/handle/10336/25894engElsevier844No. 4835Biochemical and Biophysical Research CommunicationsVol. 321Biochemical and Biophysical Research Communications, ISSN: 0006-291X;EISSN: 1090-2104, Vol.321, No.4 (2004); pp.835-844https://www.sciencedirect.com/science/article/abs/pii/S0006291X04015189Restringido (Acceso a grupos específicos)http://purl.org/coar/access_right/c_16ecBiochemical and Biophysical Research Communicationsinstname:Universidad del Rosarioreponame:Repositorio Institucional EdocURErythrocyte binding antigen-160High activity binding peptidesPlasmodium falciparumIdentifying plasmodium falciparum EBA-175 homologue sequences that specifically bind to human erythrocytesIdentificación de secuencias homólogas de Plasmodium falciparum EBA-175 que se unen específicamente a los eritrocitos humanosarticleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Valbuena, John JairoVera Bravo, RicardoLópez, RamsesRodríguez, Luis E.Curtidor, HernandoPuentes, ÁlvaroGarcía, Javier E.Tovar, DianaGómez, JohanaLeiton, JesúsPatarroyo, Manuel ElkinOcampo, Marisol10336/25894oai:repository.urosario.edu.co:10336/258942021-06-03 00:50:20.249https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co |
dc.title.spa.fl_str_mv |
Identifying plasmodium falciparum EBA-175 homologue sequences that specifically bind to human erythrocytes |
dc.title.TranslatedTitle.spa.fl_str_mv |
Identificación de secuencias homólogas de Plasmodium falciparum EBA-175 que se unen específicamente a los eritrocitos humanos |
title |
Identifying plasmodium falciparum EBA-175 homologue sequences that specifically bind to human erythrocytes |
spellingShingle |
Identifying plasmodium falciparum EBA-175 homologue sequences that specifically bind to human erythrocytes Erythrocyte binding antigen-160 High activity binding peptides Plasmodium falciparum |
title_short |
Identifying plasmodium falciparum EBA-175 homologue sequences that specifically bind to human erythrocytes |
title_full |
Identifying plasmodium falciparum EBA-175 homologue sequences that specifically bind to human erythrocytes |
title_fullStr |
Identifying plasmodium falciparum EBA-175 homologue sequences that specifically bind to human erythrocytes |
title_full_unstemmed |
Identifying plasmodium falciparum EBA-175 homologue sequences that specifically bind to human erythrocytes |
title_sort |
Identifying plasmodium falciparum EBA-175 homologue sequences that specifically bind to human erythrocytes |
dc.subject.keyword.spa.fl_str_mv |
Erythrocyte binding antigen-160 High activity binding peptides Plasmodium falciparum |
topic |
Erythrocyte binding antigen-160 High activity binding peptides Plasmodium falciparum |
description |
Erythrocyte binding antigen-160 (EBA-160) protein is a Plasmodium falciparum antigen homologue from the erythrocyte binding protein family (EBP). It has been shown that the EBP family plays a role in parasite binding to the erythrocyte surface. The EBA-160 sequence has been chemically synthesised in seventy 20-mer sequential peptides covering the entire 3D7 protein strain, each of which was tested in erythrocyte binding assays to identify possible EBA-160 functional regions. Five EBA-160 high activity binding peptides (HABPs) specifically binding to erythrocytes with high affinity were identified. Dissociation constants lay between 200 and 460 nM and Hill coefficients between 1.5 and 2.3. Erythrocyte membrane protein binding peptide cross-linking assays using SDS–PAGE showed that these peptides bound specifically to 12, 28, and 44 kDa erythrocyte membrane proteins. The nature of these receptor sites was studied in peptide binding assays using enzyme-treated erythrocytes. HABPs were able to block merozoite in vitro invasion of erythrocytes. HABPs’ potential as anti-malarial vaccine candidates is also discussed. |
publishDate |
2004 |
dc.date.created.spa.fl_str_mv |
2004-09-03 |
dc.date.accessioned.none.fl_str_mv |
2020-08-06T16:20:09Z |
dc.date.available.none.fl_str_mv |
2020-08-06T16:20:09Z |
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.2004.07.034 |
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/10336/25894 |
url |
https://doi.org/10.1016/j.bbrc.2004.07.034 https://repository.urosario.edu.co/handle/10336/25894 |
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 |
844 |
dc.relation.citationIssue.none.fl_str_mv |
No. 4 |
dc.relation.citationStartPage.none.fl_str_mv |
835 |
dc.relation.citationTitle.none.fl_str_mv |
Biochemical and Biophysical Research Communications |
dc.relation.citationVolume.none.fl_str_mv |
Vol. 321 |
dc.relation.ispartof.spa.fl_str_mv |
Biochemical and Biophysical Research Communications, ISSN: 0006-291X;EISSN: 1090-2104, Vol.321, No.4 (2004); pp.835-844 |
dc.relation.uri.spa.fl_str_mv |
https://www.sciencedirect.com/science/article/abs/pii/S0006291X04015189 |
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_ |
1831928316719792128 |