Characterisation of Plasmodium falciparum RESA-like protein peptides that bind specifically to erythrocytes and inhibit invasion
The Plasmodium falciparum ring-erythrocyte surface antigen (RESA)-like putative protein was identified and characterised. PCR and RT-PCR assays revealed that the gene encoding this protein was both present and being transcribed in P. falciparum strain FCB-2 16 h after erythrocyte invasion. Indirect...
- Autores:
- Tipo de recurso:
- Fecha de publicación:
- 2007
- Institución:
- Universidad del Rosario
- Repositorio:
- Repositorio EdocUR - U. Rosario
- Idioma:
- eng
- OAI Identifier:
- oai:repository.urosario.edu.co:10336/27352
- Acceso en línea:
- https://doi.org/10.1515/BC.2007.002
https://repository.urosario.edu.co/handle/10336/27352
- Palabra clave:
- Binding peptide
Erythrocyte
Plasmodium falciparum
RESA-like protein
- Rights
- License
- Restringido (Acceso a grupos específicos)
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Repositorio EdocUR - U. Rosario |
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45a4ad31-9f83-4647-8333-75ffd60b336b-134b82e95-53e0-4ba5-a5c5-d4191164afa1-14255e3fa-2b0d-47ce-ab18-c66a1b12d04d-191225589-1b8902bd8-16f9-4e10-84ce-847819e12c56-1eba5265c-2b9f-49a4-8c8c-4e3459a41e19-1e24a8b75-8725-433a-8f7d-b1de864249ab-12b450674-ab40-46a4-8e3b-a2e6b0ca0d5d-1353b1f84-d002-4de4-add8-a0cd9b20c19f-179653065-110ecd4f9-843f-4ef2-bec0-7d39d3381a13-1518488266002020-08-19T14:41:51Z2020-08-19T14:41:51Z2007-01-10The Plasmodium falciparum ring-erythrocyte surface antigen (RESA)-like putative protein was identified and characterised. PCR and RT-PCR assays revealed that the gene encoding this protein was both present and being transcribed in P. falciparum strain FCB-2 16 h after erythrocyte invasion. Indirect immunofluorescence studies detected this protein in infected erythrocyte (IE) cytosol in dense fluorescent granules similar to Maurer's clefts at 16–20 h (parasites in ring and trophozoite stages) and very strongly on IE membranes at 22 h, suggesting that it is synthesised during early ring stages (16 h) and transported to the infected red blood cell (RBC) membrane surface during the trophozoite stage (22 h). Western blotting showed that antisera produced against polymerised synthetic peptides of this protein recognised a 72-kDa band in P. falciparum schizont lysate. P. falciparum RESA-like peptides used in normal RBC binding assays revealed that peptides 30326 (101NAEKI LGFDD KNILE ALDLFY120), 30334 (281RVTWK KLRTK MIKAL KKSLTY300) and 30342 (431SSPQR LKFTA GGGFC GKLRNY450) bind with high activity and saturability, presenting nM affinity constants. These peptides contain ?-helical structural elements, as determined by circular dichroism, and inhibit P. falciparum in vitro invasion of normal RBCs by up to 91%, suggesting that some RESA-like protein regions are involved in intra-erythrocyte stage P. falciparum invasion.application/pdfhttps://doi.org/10.1515/BC.2007.002ISSN: 1431-6730EISSN: 1437-4315https://repository.urosario.edu.co/handle/10336/27352engWalter de Gruyter24No. 115Biological ChemistryVol. 388Biological Chemistry, ISSN: 1431-6730 ; EISSN: 1437-4315, Vol.388, No.1 (Jan 2007); pp. 15-24 https://www.degruyter.com/view/journals/bchm/388/1/article-p15.xmlRestringido (Acceso a grupos específicos)http://purl.org/coar/access_right/c_16ecBiological Chemistryinstname:Universidad del Rosarioreponame:Repositorio Institucional EdocURBinding peptideErythrocytePlasmodium falciparumRESA-like proteinCharacterisation of Plasmodium falciparum RESA-like protein peptides that bind specifically to erythrocytes and inhibit invasionCaracterización de péptidos proteicos similares a RESA de Plasmodium falciparum que se unen específicamente a eritrocitos e inhiben la invasiónarticleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Rodriguez, Luis EduardoVera, RicardoValbuena, JohnCurtidor, HernandoGarcia, JavierPuentes, AlvaroLopez, RamsesRosas, JaiverLopez, YolandaPatarroyo, Manuel A.Patarroyo, Manuel E.Ocampo, Marisol10336/27352oai:repository.urosario.edu.co:10336/273522021-06-03 00:50:11.249https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co |
dc.title.spa.fl_str_mv |
Characterisation of Plasmodium falciparum RESA-like protein peptides that bind specifically to erythrocytes and inhibit invasion |
dc.title.TranslatedTitle.spa.fl_str_mv |
Caracterización de péptidos proteicos similares a RESA de Plasmodium falciparum que se unen específicamente a eritrocitos e inhiben la invasión |
title |
Characterisation of Plasmodium falciparum RESA-like protein peptides that bind specifically to erythrocytes and inhibit invasion |
spellingShingle |
Characterisation of Plasmodium falciparum RESA-like protein peptides that bind specifically to erythrocytes and inhibit invasion Binding peptide Erythrocyte Plasmodium falciparum RESA-like protein |
title_short |
Characterisation of Plasmodium falciparum RESA-like protein peptides that bind specifically to erythrocytes and inhibit invasion |
title_full |
Characterisation of Plasmodium falciparum RESA-like protein peptides that bind specifically to erythrocytes and inhibit invasion |
title_fullStr |
Characterisation of Plasmodium falciparum RESA-like protein peptides that bind specifically to erythrocytes and inhibit invasion |
title_full_unstemmed |
Characterisation of Plasmodium falciparum RESA-like protein peptides that bind specifically to erythrocytes and inhibit invasion |
title_sort |
Characterisation of Plasmodium falciparum RESA-like protein peptides that bind specifically to erythrocytes and inhibit invasion |
dc.subject.keyword.spa.fl_str_mv |
Binding peptide Erythrocyte Plasmodium falciparum RESA-like protein |
topic |
Binding peptide Erythrocyte Plasmodium falciparum RESA-like protein |
description |
The Plasmodium falciparum ring-erythrocyte surface antigen (RESA)-like putative protein was identified and characterised. PCR and RT-PCR assays revealed that the gene encoding this protein was both present and being transcribed in P. falciparum strain FCB-2 16 h after erythrocyte invasion. Indirect immunofluorescence studies detected this protein in infected erythrocyte (IE) cytosol in dense fluorescent granules similar to Maurer's clefts at 16–20 h (parasites in ring and trophozoite stages) and very strongly on IE membranes at 22 h, suggesting that it is synthesised during early ring stages (16 h) and transported to the infected red blood cell (RBC) membrane surface during the trophozoite stage (22 h). Western blotting showed that antisera produced against polymerised synthetic peptides of this protein recognised a 72-kDa band in P. falciparum schizont lysate. P. falciparum RESA-like peptides used in normal RBC binding assays revealed that peptides 30326 (101NAEKI LGFDD KNILE ALDLFY120), 30334 (281RVTWK KLRTK MIKAL KKSLTY300) and 30342 (431SSPQR LKFTA GGGFC GKLRNY450) bind with high activity and saturability, presenting nM affinity constants. These peptides contain ?-helical structural elements, as determined by circular dichroism, and inhibit P. falciparum in vitro invasion of normal RBCs by up to 91%, suggesting that some RESA-like protein regions are involved in intra-erythrocyte stage P. falciparum invasion. |
publishDate |
2007 |
dc.date.created.spa.fl_str_mv |
2007-01-10 |
dc.date.accessioned.none.fl_str_mv |
2020-08-19T14:41:51Z |
dc.date.available.none.fl_str_mv |
2020-08-19T14:41:51Z |
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/10.1515/BC.2007.002 |
dc.identifier.issn.none.fl_str_mv |
ISSN: 1431-6730 EISSN: 1437-4315 |
dc.identifier.uri.none.fl_str_mv |
https://repository.urosario.edu.co/handle/10336/27352 |
url |
https://doi.org/10.1515/BC.2007.002 https://repository.urosario.edu.co/handle/10336/27352 |
identifier_str_mv |
ISSN: 1431-6730 EISSN: 1437-4315 |
dc.language.iso.spa.fl_str_mv |
eng |
language |
eng |
dc.relation.citationEndPage.none.fl_str_mv |
24 |
dc.relation.citationIssue.none.fl_str_mv |
No. 1 |
dc.relation.citationStartPage.none.fl_str_mv |
15 |
dc.relation.citationTitle.none.fl_str_mv |
Biological Chemistry |
dc.relation.citationVolume.none.fl_str_mv |
Vol. 388 |
dc.relation.ispartof.spa.fl_str_mv |
Biological Chemistry, ISSN: 1431-6730 ; EISSN: 1437-4315, Vol.388, No.1 (Jan 2007); pp. 15-24 |
dc.relation.uri.spa.fl_str_mv |
https://www.degruyter.com/view/journals/bchm/388/1/article-p15.xml |
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 |
Walter de Gruyter |
dc.source.spa.fl_str_mv |
Biological Chemistry |
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_ |
1831928269594689536 |