Liver stage antigen 3 Plasmodium falciparum peptides specifically interacting with HepG2 cells

Binding assays were carried out with 20 amino acid long peptides covering the complete 200-kDa Liver stage antigen (LSA) 3 protein sequence to identify its HepG2 cell binding regions. Seventeen HepG2 cell high-activity binding peptides (HABPs) were identified in the LSA-3 protein. Seven HABPs were f...

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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:10336/25974
Acceso en línea:
https://doi.org/10.1007/s00109-004-0573-9
https://repository.urosario.edu.co/handle/10336/25974
Palabra clave:
P. falciparum
Liver stage antigen-3
High activity binding peptides
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id EDOCUR2_2a7cd7a83982c90d2381f8ac110d60cf
oai_identifier_str oai:repository.urosario.edu.co:10336/25974
network_acronym_str EDOCUR2
network_name_str Repositorio EdocUR - U. Rosario
repository_id_str
spelling a4e7ff19-544a-44fe-ad9c-61d4aff3b8ba912255895e82e691-ba88-4d28-b934-b924d135083434b82e95-53e0-4ba5-a5c5-d4191164afa14255e3fa-2b0d-47ce-ab18-c66a1b12d04d2b450674-ab40-46a4-8e3b-a2e6b0ca0d5deba5265c-2b9f-49a4-8c8c-4e3459a41e1984cece1e-359c-45a6-b251-f8e4b62a84ebcb4fb759-401e-4b06-8a94-5315ca1cd40260051848826600796530656002020-08-06T16:20:21Z2020-08-06T16:20:21Z2004-09-01Binding assays were carried out with 20 amino acid long peptides covering the complete 200-kDa Liver stage antigen (LSA) 3 protein sequence to identify its HepG2 cell binding regions. Seventeen HepG2 cell high-activity binding peptides (HABPs) were identified in the LSA-3 protein. Seven HABPs were found in the nonrepeat (NRA) region A; five of these formed a 100 amino acid long HepG2 cell binding region located between residues 21Ile and 120Thr. Six HABPs were found in the R2 region and another four in the NRB2 region. LSA-3 protein HABPS bound saturably to HepG2 cells having nanomolar affinity constants and bound specifically to 31, 44, and 70 kDa HepG2 cell membrane proteins. Some of them were located in antigenic and immunogenic LSA-3 protein regions. Immunofluorescence and immunoblotting assays using goat sera immunized with LSA-3 protein peptides recognized P. falciparum (FCB-2 strain) erythrocyte stage proteins (58, 68, 72, 81, 86, 160, and 175 kDa). This reactivity was due mainly to the VEESVAEN motif present in some erythrocyte stage proteins. However, our results suggest that antibodies against LSA-3 regions had a crossed reaction with another 86-kDa protein, and that this crossed reaction was due to a motif present in the NRA region.application/pdfhttps://doi.org/10.1007/s00109-004-0573-9ISSN?: ?0946-2716EISN: 1432-1440https://repository.urosario.edu.co/handle/10336/25974engSpringer Nature611No. 9600Journal of Molecular MedicineVol. 82Journal of Molecular Medicine, ISSN?: ?0946-2716;EIISN:1432-1440, Vol.82, No.9 (September, 2004); pp.600–611https://link.springer.com/article/10.1007/s00109-004-0573-9Restringido (Acceso a grupos específicos)http://purl.org/coar/access_right/c_16ecJournal of Molecular Medicineinstname:Universidad del Rosarioreponame:Repositorio Institucional EdocURP. falciparumLiver stage antigen-3High activity binding peptidesLiver stage antigen 3 Plasmodium falciparum peptides specifically interacting with HepG2 cellsPéptidos del antígeno 3 del estadio hepático Plasmodium falciparum que interactúan específicamente con las células HepG2articleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501García, JavierCurtidor, HernandoLópez, RamsesVera, RicardoValbuena, JohnRosas, JaiverPuentes, AlvaroForero, MarthaRodriguez, LuisOcampo, MarisolPatarroyo, Manuel A.10336/25974oai:repository.urosario.edu.co:10336/259742021-11-04 15:09:06.001https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co
dc.title.spa.fl_str_mv Liver stage antigen 3 Plasmodium falciparum peptides specifically interacting with HepG2 cells
dc.title.TranslatedTitle.spa.fl_str_mv Péptidos del antígeno 3 del estadio hepático Plasmodium falciparum que interactúan específicamente con las células HepG2
title Liver stage antigen 3 Plasmodium falciparum peptides specifically interacting with HepG2 cells
spellingShingle Liver stage antigen 3 Plasmodium falciparum peptides specifically interacting with HepG2 cells
P. falciparum
Liver stage antigen-3
High activity binding peptides
title_short Liver stage antigen 3 Plasmodium falciparum peptides specifically interacting with HepG2 cells
title_full Liver stage antigen 3 Plasmodium falciparum peptides specifically interacting with HepG2 cells
title_fullStr Liver stage antigen 3 Plasmodium falciparum peptides specifically interacting with HepG2 cells
title_full_unstemmed Liver stage antigen 3 Plasmodium falciparum peptides specifically interacting with HepG2 cells
title_sort Liver stage antigen 3 Plasmodium falciparum peptides specifically interacting with HepG2 cells
dc.subject.keyword.spa.fl_str_mv P. falciparum
Liver stage antigen-3
High activity binding peptides
topic P. falciparum
Liver stage antigen-3
High activity binding peptides
description Binding assays were carried out with 20 amino acid long peptides covering the complete 200-kDa Liver stage antigen (LSA) 3 protein sequence to identify its HepG2 cell binding regions. Seventeen HepG2 cell high-activity binding peptides (HABPs) were identified in the LSA-3 protein. Seven HABPs were found in the nonrepeat (NRA) region A; five of these formed a 100 amino acid long HepG2 cell binding region located between residues 21Ile and 120Thr. Six HABPs were found in the R2 region and another four in the NRB2 region. LSA-3 protein HABPS bound saturably to HepG2 cells having nanomolar affinity constants and bound specifically to 31, 44, and 70 kDa HepG2 cell membrane proteins. Some of them were located in antigenic and immunogenic LSA-3 protein regions. Immunofluorescence and immunoblotting assays using goat sera immunized with LSA-3 protein peptides recognized P. falciparum (FCB-2 strain) erythrocyte stage proteins (58, 68, 72, 81, 86, 160, and 175 kDa). This reactivity was due mainly to the VEESVAEN motif present in some erythrocyte stage proteins. However, our results suggest that antibodies against LSA-3 regions had a crossed reaction with another 86-kDa protein, and that this crossed reaction was due to a motif present in the NRA region.
publishDate 2004
dc.date.created.spa.fl_str_mv 2004-09-01
dc.date.accessioned.none.fl_str_mv 2020-08-06T16:20:21Z
dc.date.available.none.fl_str_mv 2020-08-06T16:20:21Z
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/10.1007/s00109-004-0573-9
dc.identifier.issn.none.fl_str_mv ISSN?: ?0946-2716
EISN: 1432-1440
dc.identifier.uri.none.fl_str_mv https://repository.urosario.edu.co/handle/10336/25974
url https://doi.org/10.1007/s00109-004-0573-9
https://repository.urosario.edu.co/handle/10336/25974
identifier_str_mv ISSN?: ?0946-2716
EISN: 1432-1440
dc.language.iso.spa.fl_str_mv eng
language eng
dc.relation.citationEndPage.none.fl_str_mv 611
dc.relation.citationIssue.none.fl_str_mv No. 9
dc.relation.citationStartPage.none.fl_str_mv 600
dc.relation.citationTitle.none.fl_str_mv Journal of Molecular Medicine
dc.relation.citationVolume.none.fl_str_mv Vol. 82
dc.relation.ispartof.spa.fl_str_mv Journal of Molecular Medicine, ISSN?: ?0946-2716;EIISN:1432-1440, Vol.82, No.9 (September, 2004); pp.600–611
dc.relation.uri.spa.fl_str_mv https://link.springer.com/article/10.1007/s00109-004-0573-9
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 Springer Nature
dc.source.spa.fl_str_mv Journal of Molecular Medicine
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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