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...

Full description

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)
id EDOCUR2_b34382f9ec92cddea50f8e6a2e30fa40
oai_identifier_str oai:repository.urosario.edu.co:10336/27352
network_acronym_str EDOCUR2
network_name_str Repositorio EdocUR - U. Rosario
repository_id_str
spelling 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