Sequences of the Plasmodium falciparum cytoadherence-linked asexual protein 9 implicated in malaria parasite invasion to erythrocytes

In this study, we synthesized the complete sequence of the CLAG-9 protein as 67 20-mer-long non-overlapped peptides and assessed their ability to bind to erythrocytes in receptor-ligand assays. Twenty CLAG-9 peptides were found to have specific high-affinity binding ability to erythrocytes (thereby...

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Autores:
Tipo de recurso:
Fecha de publicación:
2010
Institución:
Universidad del Rosario
Repositorio:
Repositorio EdocUR - U. Rosario
Idioma:
eng
OAI Identifier:
oai:repository.urosario.edu.co:10336/23454
Acceso en línea:
https://doi.org/10.1016/j.vaccine.2010.01.004
https://repository.urosario.edu.co/handle/10336/23454
Palabra clave:
Cell receptor
Cytoadherence linked asexual protein 9
Protozoal protein
Unclassified drug
Amino acid sequence
Article
Binding affinity
Cell invasion
Dissociation constant
Erythrocyte
Human
Human cell
Molecular weight
Nonhuman
Plasmodium falciparum
Priority journal
Protein binding
Protein interaction
Protein synthesis
Amino acid sequence
Animals
Cell adhesion molecules
Erythrocytes
Humans
Kinetics
Membrane proteins
Molecular sequence data
Molecular weight
Peptide hydrolases
Plasmodium falciparum
Protein binding
Protozoan proteins
Virulence factors
Antimalarial vaccine
Cytoadherence-linked asexual protein 9
Plasmodium falciparum
falciparum
Malaria
Rights
License
Abierto (Texto Completo)
id EDOCUR2_bd9e69b6135ee98950458e7fec8396d9
oai_identifier_str oai:repository.urosario.edu.co:10336/23454
network_acronym_str EDOCUR2
network_name_str Repositorio EdocUR - U. Rosario
repository_id_str
spelling c45f5c54-3321-4073-9258-76a2fd84e3b7-191225589-18524e52b-4a7c-4435-9244-66a621a020c8-151721018-19de1cfc2-5d95-4925-a819-b9b2b20ff2d2-179653065-110ecd4f9-843f-4ef2-bec0-7d39d3381a13-12020-05-26T00:02:10Z2020-05-26T00:02:10Z2010In this study, we synthesized the complete sequence of the CLAG-9 protein as 67 20-mer-long non-overlapped peptides and assessed their ability to bind to erythrocytes in receptor-ligand assays. Twenty CLAG-9 peptides were found to have specific high-affinity binding ability to erythrocytes (thereby named as HABPs), with nanomolar dissociation constants. CLAG-9 HABPs interacted with different erythrocyte surface receptors having apparent molecular weights of 85, 63 and 34 kDa. CLAG-9 HABPs binding was also affected by pre-treatment of RBCs with enzymes and inhibited erythrocyte invasion in vitro by up to 72% at 200 ?M. These results suggest that some protein fragments of CLAG-9 may be part of the molecular machinery used by malaria parasites to invade erythrocytes, hence supporting their study as possible vaccine candidates. © 2010 Elsevier Ltd. All rights reserved.application/pdfhttps://doi.org/10.1016/j.vaccine.2010.01.0040264410X13588745https://repository.urosario.edu.co/handle/10336/23454eng2663No. 142653VaccineVol. 28Vaccine, ISSN:0264410X, 13588745, Vol.28, No.14 (2010); pp. 2653-2663https://www.scopus.com/inward/record.uri?eid=2-s2.0-77649180960&doi=10.1016%2fj.vaccine.2010.01.004&partnerID=40&md5=05707e9cf97d0ed0d5e8161e25678244Abierto (Texto Completo)http://purl.org/coar/access_right/c_abf2instname:Universidad del Rosarioreponame:Repositorio Institucional EdocURCell receptorCytoadherence linked asexual protein 9Protozoal proteinUnclassified drugAmino acid sequenceArticleBinding affinityCell invasionDissociation constantErythrocyteHumanHuman cellMolecular weightNonhumanPlasmodium falciparumPriority journalProtein bindingProtein interactionProtein synthesisAmino acid sequenceAnimalsCell adhesion moleculesErythrocytesHumansKineticsMembrane proteinsMolecular sequence dataMolecular weightPeptide hydrolasesPlasmodium falciparumProtein bindingProtozoan proteinsVirulence factorsAntimalarial vaccineCytoadherence-linked asexual protein 9Plasmodium falciparumfalciparumMalariaSequences of the Plasmodium falciparum cytoadherence-linked asexual protein 9 implicated in malaria parasite invasion to erythrocytesarticleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Pinzón, Carlos GiovanniCurtidor, HernandoGarcía, JeisonVanegas, MagnoliaVizcaíno, CarolinaPatarroyo, Manuel A.Patarroyo, Manuel E.10336/23454oai:repository.urosario.edu.co:10336/234542022-05-02 07:37:20.976462https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co
dc.title.spa.fl_str_mv Sequences of the Plasmodium falciparum cytoadherence-linked asexual protein 9 implicated in malaria parasite invasion to erythrocytes
title Sequences of the Plasmodium falciparum cytoadherence-linked asexual protein 9 implicated in malaria parasite invasion to erythrocytes
spellingShingle Sequences of the Plasmodium falciparum cytoadherence-linked asexual protein 9 implicated in malaria parasite invasion to erythrocytes
Cell receptor
Cytoadherence linked asexual protein 9
Protozoal protein
Unclassified drug
Amino acid sequence
Article
Binding affinity
Cell invasion
Dissociation constant
Erythrocyte
Human
Human cell
Molecular weight
Nonhuman
Plasmodium falciparum
Priority journal
Protein binding
Protein interaction
Protein synthesis
Amino acid sequence
Animals
Cell adhesion molecules
Erythrocytes
Humans
Kinetics
Membrane proteins
Molecular sequence data
Molecular weight
Peptide hydrolases
Plasmodium falciparum
Protein binding
Protozoan proteins
Virulence factors
Antimalarial vaccine
Cytoadherence-linked asexual protein 9
Plasmodium falciparum
falciparum
Malaria
title_short Sequences of the Plasmodium falciparum cytoadherence-linked asexual protein 9 implicated in malaria parasite invasion to erythrocytes
title_full Sequences of the Plasmodium falciparum cytoadherence-linked asexual protein 9 implicated in malaria parasite invasion to erythrocytes
title_fullStr Sequences of the Plasmodium falciparum cytoadherence-linked asexual protein 9 implicated in malaria parasite invasion to erythrocytes
title_full_unstemmed Sequences of the Plasmodium falciparum cytoadherence-linked asexual protein 9 implicated in malaria parasite invasion to erythrocytes
title_sort Sequences of the Plasmodium falciparum cytoadherence-linked asexual protein 9 implicated in malaria parasite invasion to erythrocytes
dc.subject.keyword.spa.fl_str_mv Cell receptor
Cytoadherence linked asexual protein 9
Protozoal protein
Unclassified drug
Amino acid sequence
Article
Binding affinity
Cell invasion
Dissociation constant
Erythrocyte
Human
Human cell
Molecular weight
Nonhuman
Plasmodium falciparum
Priority journal
Protein binding
Protein interaction
Protein synthesis
Amino acid sequence
Animals
Cell adhesion molecules
Erythrocytes
Humans
Kinetics
Membrane proteins
Molecular sequence data
Molecular weight
Peptide hydrolases
Plasmodium falciparum
Protein binding
Protozoan proteins
Virulence factors
Antimalarial vaccine
Cytoadherence-linked asexual protein 9
Plasmodium falciparum
topic Cell receptor
Cytoadherence linked asexual protein 9
Protozoal protein
Unclassified drug
Amino acid sequence
Article
Binding affinity
Cell invasion
Dissociation constant
Erythrocyte
Human
Human cell
Molecular weight
Nonhuman
Plasmodium falciparum
Priority journal
Protein binding
Protein interaction
Protein synthesis
Amino acid sequence
Animals
Cell adhesion molecules
Erythrocytes
Humans
Kinetics
Membrane proteins
Molecular sequence data
Molecular weight
Peptide hydrolases
Plasmodium falciparum
Protein binding
Protozoan proteins
Virulence factors
Antimalarial vaccine
Cytoadherence-linked asexual protein 9
Plasmodium falciparum
falciparum
Malaria
dc.subject.keyword.eng.fl_str_mv falciparum
Malaria
description In this study, we synthesized the complete sequence of the CLAG-9 protein as 67 20-mer-long non-overlapped peptides and assessed their ability to bind to erythrocytes in receptor-ligand assays. Twenty CLAG-9 peptides were found to have specific high-affinity binding ability to erythrocytes (thereby named as HABPs), with nanomolar dissociation constants. CLAG-9 HABPs interacted with different erythrocyte surface receptors having apparent molecular weights of 85, 63 and 34 kDa. CLAG-9 HABPs binding was also affected by pre-treatment of RBCs with enzymes and inhibited erythrocyte invasion in vitro by up to 72% at 200 ?M. These results suggest that some protein fragments of CLAG-9 may be part of the molecular machinery used by malaria parasites to invade erythrocytes, hence supporting their study as possible vaccine candidates. © 2010 Elsevier Ltd. All rights reserved.
publishDate 2010
dc.date.created.spa.fl_str_mv 2010
dc.date.accessioned.none.fl_str_mv 2020-05-26T00:02:10Z
dc.date.available.none.fl_str_mv 2020-05-26T00:02:10Z
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/10.1016/j.vaccine.2010.01.004
dc.identifier.issn.none.fl_str_mv 0264410X
13588745
dc.identifier.uri.none.fl_str_mv https://repository.urosario.edu.co/handle/10336/23454
url https://doi.org/10.1016/j.vaccine.2010.01.004
https://repository.urosario.edu.co/handle/10336/23454
identifier_str_mv 0264410X
13588745
dc.language.iso.spa.fl_str_mv eng
language eng
dc.relation.citationEndPage.none.fl_str_mv 2663
dc.relation.citationIssue.none.fl_str_mv No. 14
dc.relation.citationStartPage.none.fl_str_mv 2653
dc.relation.citationTitle.none.fl_str_mv Vaccine
dc.relation.citationVolume.none.fl_str_mv Vol. 28
dc.relation.ispartof.spa.fl_str_mv Vaccine, ISSN:0264410X, 13588745, Vol.28, No.14 (2010); pp. 2653-2663
dc.relation.uri.spa.fl_str_mv https://www.scopus.com/inward/record.uri?eid=2-s2.0-77649180960&doi=10.1016%2fj.vaccine.2010.01.004&partnerID=40&md5=05707e9cf97d0ed0d5e8161e25678244
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
institution Universidad del Rosario
dc.source.instname.spa.fl_str_mv instname:Universidad del Rosario
dc.source.reponame.spa.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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