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...

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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)
id EDOCUR2_99bb2b86479cbdd902540c26ab1727bd
oai_identifier_str oai:repository.urosario.edu.co:10336/27840
network_acronym_str EDOCUR2
network_name_str Repositorio EdocUR - U. Rosario
repository_id_str
spelling 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
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