Identifying Plasmodium falciparum cytoadherence-linked asexual protein 3 (CLAG 3) sequences that specifically bind to C32 cells and erythrocytes
Adhesion of mature asexual stage Plasmodium falciparum parasite-infected erythrocytes (iRBC) to thevascular endothelium is a critical event in the pathology of Plasmodium falciparum malaria. It has beensuggested that the clag gene family is essential in cytoadherence to endothelial receptors. Primer...
- 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:10336/27840
- Acceso en línea:
- https://doi.org/10.1110/ps.04883905
https://repository.urosario.edu.co/handle/10336/27840
- Palabra clave:
- Plasmodium falciparum
Cytoadherence
C32 cells
Peptides
CLAG
cytoadherence?linked asexual protein
HABPs
high activity binding peptides
PRBCs
parasitized red blood cells HBS
HEPES buffered saline
- Rights
- License
- Abierto (Texto Completo)
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oai:repository.urosario.edu.co:10336/27840 |
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EDOCUR2 |
network_name_str |
Repositorio EdocUR - U. Rosario |
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51848826600ef6547b6-3130-435a-8a09-7ca050cd7b64-191225589-1f2d05f42-2948-4c51-8389-8c3817c2d0f1-134b82e95-53e0-4ba5-a5c5-d4191164afa1-12020-08-19T14:44:10Z2020-08-19T14:44:10Z2005-02Adhesion of mature asexual stage Plasmodium falciparum parasite-infected erythrocytes (iRBC) to thevascular endothelium is a critical event in the pathology of Plasmodium falciparum malaria. It has beensuggested that the clag gene family is essential in cytoadherence to endothelial receptors. Primers used inPCR and RT-PCR assays allowed us to determine that the gene encoding CLAG 3 (GenBank accession no.NP_473155) is transcribed in the Plasmodium falciparum FCB2 strain. Western blot showed that antiseraproduced against polymerized synthetic peptides from this protein recognized a 142-kDa band in P. falci-parum schizont lysate. Seventy-one 20-amino-acid-long nonoverlapping peptides, spanning the CLAG 3(cytoadherence-linked asexual protein on chromosome 3) sequence were tested in C32 cell and erythrocytebinding assays. Twelve CLAG peptides specifically bound to C32 cells (which mainly express CD36) withhigh affinity, hereafter referred to as high-affinity binding peptides (HABPs). Five of them also bound toerythrocytes. HABP binding to C32 cells and erythrocytes was independent of peptide charge or peptidestructure. Affinity constants were between 100 nM and 800 nM. Cross-linking and SDS-PAGE analysisallowed two erythrocyte binding proteins of around 26 kDa and 59 kDa to be identified, while proteins ofaround 53 kDa were identified as possible receptor sites for C-32 cells. The HABPs’ role in Plasmodiumfalciparum invasion inhibition was determined. Such an approach analyzing various CLAG 3 regions mayelucidate their functions and may help in the search for new antigens important for developing antimalarialvaccines.application/pdfhttps://doi.org/10.1110/ps.04883905ISSN: 0961-8368EISSN: 1469-896Xhttps://repository.urosario.edu.co/handle/10336/27840engThe Protein SocietyJohn Wiley & Son513No. 2504Protein ScienceVol. 14Protein Science, ISSN: 0961-8368;EISSN: 1469-896X, Vol.14, No.2 (February 2005); pp. 504-513https://onlinelibrary.wiley.com/doi/epdf/10.1110/ps.04883905Abierto (Texto Completo)http://purl.org/coar/access_right/c_abf2Protein Scienceinstname:Universidad del Rosarioreponame:Repositorio Institucional EdocURPlasmodium falciparumCytoadherenceC32 cellsPeptidesCLAGcytoadherence?linked asexual proteinHABPshigh activity binding peptidesPRBCsparasitized red blood cells HBSHEPES buffered salineIdentifying Plasmodium falciparum cytoadherence-linked asexual protein 3 (CLAG 3) sequences that specifically bind to C32 cells and erythrocytesIdentificación de secuencias de la proteína asexual 3 unida por citoadherencia de Plasmodium falciparum (CLAG 3) que se unen específicamente a células C32 y eritrocitosarticleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Ocampo, MarisolRodríguez, Luis E.Curtidor, HernandoPuentes, ÁlvaroVera, Ricardo10336/27840oai:repository.urosario.edu.co:10336/278402021-06-03 00:51:03.495https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co |
dc.title.spa.fl_str_mv |
Identifying Plasmodium falciparum cytoadherence-linked asexual protein 3 (CLAG 3) sequences that specifically bind to C32 cells and erythrocytes |
dc.title.TranslatedTitle.spa.fl_str_mv |
Identificación de secuencias de la proteína asexual 3 unida por citoadherencia de Plasmodium falciparum (CLAG 3) que se unen específicamente a células C32 y eritrocitos |
title |
Identifying Plasmodium falciparum cytoadherence-linked asexual protein 3 (CLAG 3) sequences that specifically bind to C32 cells and erythrocytes |
spellingShingle |
Identifying Plasmodium falciparum cytoadherence-linked asexual protein 3 (CLAG 3) sequences that specifically bind to C32 cells and erythrocytes Plasmodium falciparum Cytoadherence C32 cells Peptides CLAG cytoadherence?linked asexual protein HABPs high activity binding peptides PRBCs parasitized red blood cells HBS HEPES buffered saline |
title_short |
Identifying Plasmodium falciparum cytoadherence-linked asexual protein 3 (CLAG 3) sequences that specifically bind to C32 cells and erythrocytes |
title_full |
Identifying Plasmodium falciparum cytoadherence-linked asexual protein 3 (CLAG 3) sequences that specifically bind to C32 cells and erythrocytes |
title_fullStr |
Identifying Plasmodium falciparum cytoadherence-linked asexual protein 3 (CLAG 3) sequences that specifically bind to C32 cells and erythrocytes |
title_full_unstemmed |
Identifying Plasmodium falciparum cytoadherence-linked asexual protein 3 (CLAG 3) sequences that specifically bind to C32 cells and erythrocytes |
title_sort |
Identifying Plasmodium falciparum cytoadherence-linked asexual protein 3 (CLAG 3) sequences that specifically bind to C32 cells and erythrocytes |
dc.subject.keyword.spa.fl_str_mv |
Plasmodium falciparum Cytoadherence C32 cells Peptides CLAG cytoadherence?linked asexual protein HABPs high activity binding peptides PRBCs parasitized red blood cells HBS HEPES buffered saline |
topic |
Plasmodium falciparum Cytoadherence C32 cells Peptides CLAG cytoadherence?linked asexual protein HABPs high activity binding peptides PRBCs parasitized red blood cells HBS HEPES buffered saline |
description |
Adhesion of mature asexual stage Plasmodium falciparum parasite-infected erythrocytes (iRBC) to thevascular endothelium is a critical event in the pathology of Plasmodium falciparum malaria. It has beensuggested that the clag gene family is essential in cytoadherence to endothelial receptors. Primers used inPCR and RT-PCR assays allowed us to determine that the gene encoding CLAG 3 (GenBank accession no.NP_473155) is transcribed in the Plasmodium falciparum FCB2 strain. Western blot showed that antiseraproduced against polymerized synthetic peptides from this protein recognized a 142-kDa band in P. falci-parum schizont lysate. Seventy-one 20-amino-acid-long nonoverlapping peptides, spanning the CLAG 3(cytoadherence-linked asexual protein on chromosome 3) sequence were tested in C32 cell and erythrocytebinding assays. Twelve CLAG peptides specifically bound to C32 cells (which mainly express CD36) withhigh affinity, hereafter referred to as high-affinity binding peptides (HABPs). Five of them also bound toerythrocytes. HABP binding to C32 cells and erythrocytes was independent of peptide charge or peptidestructure. Affinity constants were between 100 nM and 800 nM. Cross-linking and SDS-PAGE analysisallowed two erythrocyte binding proteins of around 26 kDa and 59 kDa to be identified, while proteins ofaround 53 kDa were identified as possible receptor sites for C-32 cells. The HABPs’ role in Plasmodiumfalciparum invasion inhibition was determined. Such an approach analyzing various CLAG 3 regions mayelucidate their functions and may help in the search for new antigens important for developing antimalarialvaccines. |
publishDate |
2005 |
dc.date.created.spa.fl_str_mv |
2005-02 |
dc.date.accessioned.none.fl_str_mv |
2020-08-19T14:44:10Z |
dc.date.available.none.fl_str_mv |
2020-08-19T14:44:10Z |
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/10.1110/ps.04883905 |
dc.identifier.issn.none.fl_str_mv |
ISSN: 0961-8368 EISSN: 1469-896X |
dc.identifier.uri.none.fl_str_mv |
https://repository.urosario.edu.co/handle/10336/27840 |
url |
https://doi.org/10.1110/ps.04883905 https://repository.urosario.edu.co/handle/10336/27840 |
identifier_str_mv |
ISSN: 0961-8368 EISSN: 1469-896X |
dc.language.iso.spa.fl_str_mv |
eng |
language |
eng |
dc.relation.citationEndPage.none.fl_str_mv |
513 |
dc.relation.citationIssue.none.fl_str_mv |
No. 2 |
dc.relation.citationStartPage.none.fl_str_mv |
504 |
dc.relation.citationTitle.none.fl_str_mv |
Protein Science |
dc.relation.citationVolume.none.fl_str_mv |
Vol. 14 |
dc.relation.ispartof.spa.fl_str_mv |
Protein Science, ISSN: 0961-8368;EISSN: 1469-896X, Vol.14, No.2 (February 2005); pp. 504-513 |
dc.relation.uri.spa.fl_str_mv |
https://onlinelibrary.wiley.com/doi/epdf/10.1110/ps.04883905 |
dc.rights.coar.fl_str_mv |
http://purl.org/coar/access_right/c_abf2 |
dc.rights.acceso.spa.fl_str_mv |
Abierto (Texto Completo) |
rights_invalid_str_mv |
Abierto (Texto Completo) http://purl.org/coar/access_right/c_abf2 |
dc.format.mimetype.none.fl_str_mv |
application/pdf |
dc.publisher.spa.fl_str_mv |
The Protein Society John Wiley & Son |
dc.source.spa.fl_str_mv |
Protein Science |
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_ |
1814167525746802688 |