MAEBL Plasmodium falciparum protein peptides bind specifically to erythrocytes and inhibit in vitro merozoite invasion
MAEBL is an erythrocyte binding protein located in the rhoptries and on the surface of mature merozoites, being expressed at the beginning of schizogony. The structure of MAEBL originally isolated from rodent malaria parasites suggested a molecule likely to be involved in invasion. We thus became 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:10336/25933
- Acceso en línea:
- https://doi.org/10.1016/j.bbrc.2004.01.050
https://repository.urosario.edu.co/handle/10336/25933
- Palabra clave:
- MAEBL
Peptides
Malaria
- Rights
- License
- Restringido (Acceso a grupos específicos)
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Repositorio EdocUR - U. Rosario |
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a3fe0f4d-e232-48fd-9979-2482470afb57-191225589-134b82e95-53e0-4ba5-a5c5-d4191164afa1-1bbc66b15-6431-42e4-ae1d-915ec7a26072-1efc03fc3-85c7-4fd4-b781-5082e60208ef-1f2d05f42-2948-4c51-8389-8c3817c2d0f1-15e82e691-ba88-4d28-b934-b924d1350834-1d955461b-ddf3-4124-87c6-4ae101d2757d-1fa33b517-50cf-4bb5-a980-3773caf84cd8-12f683c4a-0235-4316-879b-426a6cb8ebfc-1ff4ed10c-7d44-4208-9ba0-cc1b258b3fa9-110ecd4f9-843f-4ef2-bec0-7d39d3381a13-12020-08-06T16:20:15Z2020-08-06T16:20:15Z2004-03-05MAEBL is an erythrocyte binding protein located in the rhoptries and on the surface of mature merozoites, being expressed at the beginning of schizogony. The structure of MAEBL originally isolated from rodent malaria parasites suggested a molecule likely to be involved in invasion. We thus became interested in identifying possible MAEBL functional regions. Synthetic peptides spanning the MAEBL sequence were tested in erythrocyte binding assays to identify such possible MAEBL functional regions. Nine high activity binding peptides (HABPs) were identified: two were found in the M1 domain, one was found between the M1 and M2 regions, five in the erythrocyte binding domain (M2), and one in the protein’s repeat region. The results showed that peptide binding was saturable; some HABPs inhibited in vitro merozoite invasion and specifically bound to a 33 kDa protein on red blood cell membrane. HABPs’ possible function in merozoite invasion of erythrocytes is also discussed.application/pdfhttps://doi.org/10.1016/j.bbrc.2004.01.050ISSN: 0006-291XEISSN: 1090-2104https://repository.urosario.edu.co/handle/10336/25933engElsevier329No. 2319Biochemical and Biophysical Research CommunicationsVol. 315Biochemical and Biophysical Research Communications, ISSN: 0006-291X;EISSN: 1090-2104, Vol.315, No.2 (2004); pp.319-329https://www.sciencedirect.com/science/article/abs/pii/S0006291X04000920Restringido (Acceso a grupos específicos)http://purl.org/coar/access_right/c_16ecBiochemical and Biophysical Research Communicationsinstname:Universidad del Rosarioreponame:Repositorio Institucional EdocURMAEBLPeptidesMalariaMAEBL Plasmodium falciparum protein peptides bind specifically to erythrocytes and inhibit in vitro merozoite invasionLos péptidos de proteína MAEBL Plasmodium falciparum se unen específicamente a los eritrocitos e inhiben la invasión in vitro de merozoitosarticleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Ocampo,MarisolCurtidor, HernandoVera, RicardoValbuena, John J.Rodr??guez, Luis E.Puentes, ÁlvaroLópez, RamsesGarc??a, Javier E.Tovar, DianaPacheco, PaolaNavarro, Miguel A.Patarroyo, Manuel E.10336/25933oai:repository.urosario.edu.co:10336/259332022-05-02 07:37:21.732023https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co |
dc.title.spa.fl_str_mv |
MAEBL Plasmodium falciparum protein peptides bind specifically to erythrocytes and inhibit in vitro merozoite invasion |
dc.title.TranslatedTitle.eng.fl_str_mv |
Los péptidos de proteína MAEBL Plasmodium falciparum se unen específicamente a los eritrocitos e inhiben la invasión in vitro de merozoitos |
title |
MAEBL Plasmodium falciparum protein peptides bind specifically to erythrocytes and inhibit in vitro merozoite invasion |
spellingShingle |
MAEBL Plasmodium falciparum protein peptides bind specifically to erythrocytes and inhibit in vitro merozoite invasion MAEBL Peptides Malaria |
title_short |
MAEBL Plasmodium falciparum protein peptides bind specifically to erythrocytes and inhibit in vitro merozoite invasion |
title_full |
MAEBL Plasmodium falciparum protein peptides bind specifically to erythrocytes and inhibit in vitro merozoite invasion |
title_fullStr |
MAEBL Plasmodium falciparum protein peptides bind specifically to erythrocytes and inhibit in vitro merozoite invasion |
title_full_unstemmed |
MAEBL Plasmodium falciparum protein peptides bind specifically to erythrocytes and inhibit in vitro merozoite invasion |
title_sort |
MAEBL Plasmodium falciparum protein peptides bind specifically to erythrocytes and inhibit in vitro merozoite invasion |
dc.subject.keyword.spa.fl_str_mv |
MAEBL Peptides Malaria |
topic |
MAEBL Peptides Malaria |
description |
MAEBL is an erythrocyte binding protein located in the rhoptries and on the surface of mature merozoites, being expressed at the beginning of schizogony. The structure of MAEBL originally isolated from rodent malaria parasites suggested a molecule likely to be involved in invasion. We thus became interested in identifying possible MAEBL functional regions. Synthetic peptides spanning the MAEBL sequence were tested in erythrocyte binding assays to identify such possible MAEBL functional regions. Nine high activity binding peptides (HABPs) were identified: two were found in the M1 domain, one was found between the M1 and M2 regions, five in the erythrocyte binding domain (M2), and one in the protein’s repeat region. The results showed that peptide binding was saturable; some HABPs inhibited in vitro merozoite invasion and specifically bound to a 33 kDa protein on red blood cell membrane. HABPs’ possible function in merozoite invasion of erythrocytes is also discussed. |
publishDate |
2004 |
dc.date.created.spa.fl_str_mv |
2004-03-05 |
dc.date.accessioned.none.fl_str_mv |
2020-08-06T16:20:15Z |
dc.date.available.none.fl_str_mv |
2020-08-06T16:20:15Z |
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.2004.01.050 |
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/10336/25933 |
url |
https://doi.org/10.1016/j.bbrc.2004.01.050 https://repository.urosario.edu.co/handle/10336/25933 |
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 |
329 |
dc.relation.citationIssue.none.fl_str_mv |
No. 2 |
dc.relation.citationStartPage.none.fl_str_mv |
319 |
dc.relation.citationTitle.none.fl_str_mv |
Biochemical and Biophysical Research Communications |
dc.relation.citationVolume.none.fl_str_mv |
Vol. 315 |
dc.relation.ispartof.spa.fl_str_mv |
Biochemical and Biophysical Research Communications, ISSN: 0006-291X;EISSN: 1090-2104, Vol.315, No.2 (2004); pp.319-329 |
dc.relation.uri.spa.fl_str_mv |
https://www.sciencedirect.com/science/article/abs/pii/S0006291X04000920 |
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_ |
1831928289656045568 |