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

Carlos Giovanni Pinzón, Hernando Curtidor, Jeison García, Magnolia Vanegas, Carolina Vizcaíno, Manuel A. Patarroyo, Manuel E. Patarroyo

Resultado de la investigación: Contribución a RevistaArtículo

6 Citas (Scopus)

Resumen

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 μM. 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.
Idioma originalEnglish (US)
Páginas (desde-hasta)2653-2663
Número de páginas11
PublicaciónVaccine
DOI
EstadoPublished - mar 19 2010

Huella dactilar

Plasmodium falciparum
cell adhesion
malaria
Malaria
Parasites
erythrocytes
Erythrocytes
parasites
Proteins
proteins
Peptides
peptides
receptors
binding capacity
Vaccines
Molecular Weight
Ligands
pretreatment
molecular weight
vaccines

Citar esto

Pinzón, Carlos Giovanni ; Curtidor, Hernando ; García, Jeison ; Vanegas, Magnolia ; Vizcaíno, Carolina ; Patarroyo, Manuel A. ; Patarroyo, Manuel E. / Sequences of the Plasmodium falciparum cytoadherence-linked asexual protein 9 implicated in malaria parasite invasion to erythrocytes. En: Vaccine. 2010 ; pp. 2653-2663.
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title = "Sequences of the Plasmodium falciparum cytoadherence-linked asexual protein 9 implicated in malaria parasite invasion to erythrocytes",
abstract = "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 μM. 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. {\circledC} 2010 Elsevier Ltd. All rights reserved.",
author = "Pinz{\'o}n, {Carlos Giovanni} and Hernando Curtidor and Jeison Garc{\'i}a and Magnolia Vanegas and Carolina Vizca{\'i}no and Patarroyo, {Manuel A.} and Patarroyo, {Manuel E.}",
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Sequences of the Plasmodium falciparum cytoadherence-linked asexual protein 9 implicated in malaria parasite invasion to erythrocytes. / Pinzón, Carlos Giovanni; Curtidor, Hernando; García, Jeison; Vanegas, Magnolia; Vizcaíno, Carolina; Patarroyo, Manuel A.; Patarroyo, Manuel E.

En: Vaccine, 19.03.2010, p. 2653-2663.

Resultado de la investigación: Contribución a RevistaArtículo

TY - JOUR

T1 - Sequences of the Plasmodium falciparum cytoadherence-linked asexual protein 9 implicated in malaria parasite invasion to erythrocytes

AU - Pinzón, Carlos Giovanni

AU - Curtidor, Hernando

AU - García, Jeison

AU - Vanegas, Magnolia

AU - Vizcaíno, Carolina

AU - Patarroyo, Manuel A.

AU - Patarroyo, Manuel E.

PY - 2010/3/19

Y1 - 2010/3/19

N2 - 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 μM. 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.

AB - 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 μM. 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.

U2 - 10.1016/j.vaccine.2010.01.004

DO - 10.1016/j.vaccine.2010.01.004

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JO - Vaccine

JF - Vaccine

SN - 0264-410X

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