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...

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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
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License
Restringido (Acceso a grupos específicos)
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oai_identifier_str oai:repository.urosario.edu.co:10336/25933
network_acronym_str EDOCUR2
network_name_str Repositorio EdocUR - U. Rosario
repository_id_str
spelling 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
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