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...

Full description

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)
id EDOCUR2_31621090d8f4516562b24bd7cfceb6f9
oai_identifier_str oai:repository.urosario.edu.co:10336/25894
network_acronym_str EDOCUR2
network_name_str Repositorio EdocUR - U. Rosario
repository_id_str
spelling 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