Peptides from the plasmodium falciparum STEVOR putative protein bind with high affinity to normal human red blood cells

Synthetic 20-mer long non-overlapped peptides, from STEVOR protein, were tested in RBC binding assays for identifying STEVOR protein regions having high RBC binding activity and evaluating whether these regions inhibit Plasmodium falciparum in vitro invasion. Affinity constants, binding site number...

Full description

Autores:
Tipo de recurso:
Fecha de publicación:
2005
Institución:
Universidad del Rosario
Repositorio:
Repositorio EdocUR - U. Rosario
Idioma:
eng
OAI Identifier:
oai:repository.urosario.edu.co:10336/26703
Acceso en línea:
https://doi.org/10.1016/j.peptides.2005.01.013
https://repository.urosario.edu.co/handle/10336/26703
Palabra clave:
P. falciparum
STEVOR
High activity binding peptides
Rights
License
Restringido (Acceso a grupos específicos)
id EDOCUR2_f64ebe771b461a39ba62b9c3d0b1400a
oai_identifier_str oai:repository.urosario.edu.co:10336/26703
network_acronym_str EDOCUR2
network_name_str Repositorio EdocUR - U. Rosario
repository_id_str
spelling a650efd0-af5f-4ce9-9620-e1cad93a9173eba5265c-2b9f-49a4-8c8c-4e3459a41e199122558934b82e95-53e0-4ba5-a5c5-d4191164afa14255e3fa-2b0d-47ce-ab18-c66a1b12d04d5e82e691-ba88-4d28-b934-b924d1350834d191987c-6e13-4f7f-88bd-c34b437b85c6517210182b450674-ab40-46a4-8e3b-a2e6b0ca0d5d6fc431a4-2889-4e78-ba01-10c2807c655710ecd4f9-843f-4ef2-bec0-7d39d3381a13cb4fb759-401e-4b06-8a94-5315ca1cd402600518488266002020-08-19T14:40:05Z2020-08-19T14:40:05Z2005-07-01Synthetic 20-mer long non-overlapped peptides, from STEVOR protein, were tested in RBC binding assays for identifying STEVOR protein regions having high RBC binding activity and evaluating whether these regions inhibit Plasmodium falciparum in vitro invasion. Affinity constants, binding site number per cell and Hill coefficients were determined by saturation assay with high activity binding peptides (HABPs). HABP binding assays using RBCs previously treated with enzymes were carried out to study the nature of the receptor. The molecular weight of RBC surface proteins interacting with HABPs was determined by cross-linking assays and SDS-PAGE analysis. RBC binding assays revealed that peptides 30561 (41MKSRRLAEIQLPKCPHYNND60), 30562 (61PELKKIIDKLNEERIKKYIE80) and 30567 (161ASCCKVHDNYLDNLKKGCFG180) bound saturably and with high binding activity, presenting nanomolar affinity constants. HABP binding activity to RBCs previously treated with neuraminidase and trypsin decreased, suggesting that these peptides bound to RBC surface proteins and that such binding could be sialic acid dependent. Cross-linking and SDS-PAGE assays showed that the three HABPs specifically bound to 30 and 40 kDa molecular weight RBC membrane proteins. Peptides 30561, 30562 and 30567 inhibited P. falciparum in vitro invasion of red blood cells in a concentration-dependent way. Goat sera having STEVOR protein polymeric peptides antibodies inhibit parasite in vitro invasion depending on concentration. Three peptides localized in STEVOR N-terminal and central regions had high, saturable, binding activity to 30 and 40 kDa RBC membrane proteins. These peptides inhibited the parasite's in vitro invasion, suggesting that STEVOR protein regions are involved in P. falciparum invasion processes during intra-erythrocyte stage.application/pdfhttps://doi.org/10.1016/j.peptides.2005.01.013ISSN: 0196-9781EISSN: 1873-5169https://repository.urosario.edu.co/handle/10336/26703engElsevier1143No. 71133PeptidesVol. 26Peptides, ISSN: 0196-9781;EISSN: 1873-5169, Vol.26, No.7 (2005); pp. 1133-1143https://www.sciencedirect.com/science/article/abs/pii/S0196978105000276Restringido (Acceso a grupos específicos)http://purl.org/coar/access_right/c_16ecPeptidesinstname:Universidad del Rosarioreponame:Repositorio Institucional EdocURP. falciparumSTEVORHigh activity binding peptidesPeptides from the plasmodium falciparum STEVOR putative protein bind with high affinity to normal human red blood cellsPeptides from the plasmodium falciparum STEVOR putative protein bind with high affinity to normal human red blood cellsarticleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501García, Javier E.Puentes, AlvaroCurtidor, HernandoVera, RicardoValbuena, JohnLópez, RamsesCortés, JimenaVanegas, MagnoliaRosas, JaiverReyes, ClaudiaPatarroyo, Manuel E.Rodríguez, LuisOcampo, Marisol10336/26703oai:repository.urosario.edu.co:10336/267032021-11-04 15:20:54.23https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co
dc.title.spa.fl_str_mv Peptides from the plasmodium falciparum STEVOR putative protein bind with high affinity to normal human red blood cells
dc.title.alternative.spa.fl_str_mv Peptides from the plasmodium falciparum STEVOR putative protein bind with high affinity to normal human red blood cells
title Peptides from the plasmodium falciparum STEVOR putative protein bind with high affinity to normal human red blood cells
spellingShingle Peptides from the plasmodium falciparum STEVOR putative protein bind with high affinity to normal human red blood cells
P. falciparum
STEVOR
High activity binding peptides
title_short Peptides from the plasmodium falciparum STEVOR putative protein bind with high affinity to normal human red blood cells
title_full Peptides from the plasmodium falciparum STEVOR putative protein bind with high affinity to normal human red blood cells
title_fullStr Peptides from the plasmodium falciparum STEVOR putative protein bind with high affinity to normal human red blood cells
title_full_unstemmed Peptides from the plasmodium falciparum STEVOR putative protein bind with high affinity to normal human red blood cells
title_sort Peptides from the plasmodium falciparum STEVOR putative protein bind with high affinity to normal human red blood cells
dc.subject.keyword.spa.fl_str_mv P. falciparum
STEVOR
High activity binding peptides
topic P. falciparum
STEVOR
High activity binding peptides
description Synthetic 20-mer long non-overlapped peptides, from STEVOR protein, were tested in RBC binding assays for identifying STEVOR protein regions having high RBC binding activity and evaluating whether these regions inhibit Plasmodium falciparum in vitro invasion. Affinity constants, binding site number per cell and Hill coefficients were determined by saturation assay with high activity binding peptides (HABPs). HABP binding assays using RBCs previously treated with enzymes were carried out to study the nature of the receptor. The molecular weight of RBC surface proteins interacting with HABPs was determined by cross-linking assays and SDS-PAGE analysis. RBC binding assays revealed that peptides 30561 (41MKSRRLAEIQLPKCPHYNND60), 30562 (61PELKKIIDKLNEERIKKYIE80) and 30567 (161ASCCKVHDNYLDNLKKGCFG180) bound saturably and with high binding activity, presenting nanomolar affinity constants. HABP binding activity to RBCs previously treated with neuraminidase and trypsin decreased, suggesting that these peptides bound to RBC surface proteins and that such binding could be sialic acid dependent. Cross-linking and SDS-PAGE assays showed that the three HABPs specifically bound to 30 and 40 kDa molecular weight RBC membrane proteins. Peptides 30561, 30562 and 30567 inhibited P. falciparum in vitro invasion of red blood cells in a concentration-dependent way. Goat sera having STEVOR protein polymeric peptides antibodies inhibit parasite in vitro invasion depending on concentration. Three peptides localized in STEVOR N-terminal and central regions had high, saturable, binding activity to 30 and 40 kDa RBC membrane proteins. These peptides inhibited the parasite's in vitro invasion, suggesting that STEVOR protein regions are involved in P. falciparum invasion processes during intra-erythrocyte stage.
publishDate 2005
dc.date.created.spa.fl_str_mv 2005-07-01
dc.date.accessioned.none.fl_str_mv 2020-08-19T14:40:05Z
dc.date.available.none.fl_str_mv 2020-08-19T14:40:05Z
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.peptides.2005.01.013
dc.identifier.issn.none.fl_str_mv ISSN: 0196-9781
EISSN: 1873-5169
dc.identifier.uri.none.fl_str_mv https://repository.urosario.edu.co/handle/10336/26703
url https://doi.org/10.1016/j.peptides.2005.01.013
https://repository.urosario.edu.co/handle/10336/26703
identifier_str_mv ISSN: 0196-9781
EISSN: 1873-5169
dc.language.iso.spa.fl_str_mv eng
language eng
dc.relation.citationEndPage.none.fl_str_mv 1143
dc.relation.citationIssue.none.fl_str_mv No. 7
dc.relation.citationStartPage.none.fl_str_mv 1133
dc.relation.citationTitle.none.fl_str_mv Peptides
dc.relation.citationVolume.none.fl_str_mv Vol. 26
dc.relation.ispartof.spa.fl_str_mv Peptides, ISSN: 0196-9781;EISSN: 1873-5169, Vol.26, No.7 (2005); pp. 1133-1143
dc.relation.uri.spa.fl_str_mv https://www.sciencedirect.com/science/article/abs/pii/S0196978105000276
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 Peptides
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_ 1808390618135658496