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...
- 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)
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oai:repository.urosario.edu.co:10336/23454 |
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EDOCUR2 |
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Repositorio EdocUR - U. Rosario |
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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 |
_version_ |
1814167492929519616 |