Synthetic peptides from conserved regions of the Plasmodium falciparum early transcribed membrane and ring exported proteins bind specifically to red blood cell proteins

Jeison Garcia, Hernando Curtidor, Ana Z. Obando-Martinez, Carolina Vizcaíno, Martha Pinto, Nora L. Martinez, Manuel A. Patarroyo, Manuel E. Patarroyo

Resultado de la investigación: Contribución a RevistaArtículo

7 Citas (Scopus)

Resumen

Severe malaria pathology is directly associated with cytoadherence of infected red blood cells (iRBCs) to healthy RBCs and/or endothelial cells occurring during the intraerythrocytic development of Plasmodium falciparum. We synthesized, as 20-mer long peptides, the members of the ring exported (REX) protein family encoded in chromosome 9, as well as the early transcribed membrane proteins (E-TRAMP) 10.2 and 4, to identify specific RBC binding regions in these proteins. Twelve binding peptides were identified (designated as HABPs): three were identified in REX1, two in REX2, one in REX3, two in REX4 and four in E-TRAMP 10.2. The majority of these HABPs was conserved among different P. falciparum strains, according to sequence analysis. No HABPs were found in E-TRAMP 4. Bindings of HABPs were saturable and sensitive to the enzymatic treatment of RBCs and HABPs had different structural features, according to circular dichroism studies. Our results suggest that the REX and E-TRAMP families participate in relevant interactions with RBC membrane proteins, which highlight these proteins as potential targets for the development of fully effective immunoprophylactic methods. © 2009 Elsevier Ltd. All rights reserved.
Idioma originalEnglish (US)
Páginas (desde-hasta)6877-6886
Número de páginas10
PublicaciónVaccine
DOI
EstadoPublished - nov 16 2009

Huella dactilar

synthetic peptides
Plasmodium falciparum
membrane proteins
Blood Proteins
Membrane Proteins
erythrocytes
Erythrocytes
Peptides
Membranes
Proteins
proteins
peptides
circular dichroism spectroscopy
Chromosomes, Human, Pair 9
enzymatic treatment
Circular Dichroism
cell adhesion
malaria
endothelial cells
Malaria

Citar esto

Garcia, Jeison ; Curtidor, Hernando ; Obando-Martinez, Ana Z. ; Vizcaíno, Carolina ; Pinto, Martha ; Martinez, Nora L. ; Patarroyo, Manuel A. ; Patarroyo, Manuel E. / Synthetic peptides from conserved regions of the Plasmodium falciparum early transcribed membrane and ring exported proteins bind specifically to red blood cell proteins. En: Vaccine. 2009 ; pp. 6877-6886.
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title = "Synthetic peptides from conserved regions of the Plasmodium falciparum early transcribed membrane and ring exported proteins bind specifically to red blood cell proteins",
abstract = "Severe malaria pathology is directly associated with cytoadherence of infected red blood cells (iRBCs) to healthy RBCs and/or endothelial cells occurring during the intraerythrocytic development of Plasmodium falciparum. We synthesized, as 20-mer long peptides, the members of the ring exported (REX) protein family encoded in chromosome 9, as well as the early transcribed membrane proteins (E-TRAMP) 10.2 and 4, to identify specific RBC binding regions in these proteins. Twelve binding peptides were identified (designated as HABPs): three were identified in REX1, two in REX2, one in REX3, two in REX4 and four in E-TRAMP 10.2. The majority of these HABPs was conserved among different P. falciparum strains, according to sequence analysis. No HABPs were found in E-TRAMP 4. Bindings of HABPs were saturable and sensitive to the enzymatic treatment of RBCs and HABPs had different structural features, according to circular dichroism studies. Our results suggest that the REX and E-TRAMP families participate in relevant interactions with RBC membrane proteins, which highlight these proteins as potential targets for the development of fully effective immunoprophylactic methods. {\circledC} 2009 Elsevier Ltd. All rights reserved.",
author = "Jeison Garcia and Hernando Curtidor and Obando-Martinez, {Ana Z.} and Carolina Vizca{\'i}no and Martha Pinto and Martinez, {Nora L.} and Patarroyo, {Manuel A.} and Patarroyo, {Manuel E.}",
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Synthetic peptides from conserved regions of the Plasmodium falciparum early transcribed membrane and ring exported proteins bind specifically to red blood cell proteins. / Garcia, Jeison; Curtidor, Hernando; Obando-Martinez, Ana Z.; Vizcaíno, Carolina; Pinto, Martha; Martinez, Nora L.; Patarroyo, Manuel A.; Patarroyo, Manuel E.

En: Vaccine, 16.11.2009, p. 6877-6886.

Resultado de la investigación: Contribución a RevistaArtículo

TY - JOUR

T1 - Synthetic peptides from conserved regions of the Plasmodium falciparum early transcribed membrane and ring exported proteins bind specifically to red blood cell proteins

AU - Garcia, Jeison

AU - Curtidor, Hernando

AU - Obando-Martinez, Ana Z.

AU - Vizcaíno, Carolina

AU - Pinto, Martha

AU - Martinez, Nora L.

AU - Patarroyo, Manuel A.

AU - Patarroyo, Manuel E.

PY - 2009/11/16

Y1 - 2009/11/16

N2 - Severe malaria pathology is directly associated with cytoadherence of infected red blood cells (iRBCs) to healthy RBCs and/or endothelial cells occurring during the intraerythrocytic development of Plasmodium falciparum. We synthesized, as 20-mer long peptides, the members of the ring exported (REX) protein family encoded in chromosome 9, as well as the early transcribed membrane proteins (E-TRAMP) 10.2 and 4, to identify specific RBC binding regions in these proteins. Twelve binding peptides were identified (designated as HABPs): three were identified in REX1, two in REX2, one in REX3, two in REX4 and four in E-TRAMP 10.2. The majority of these HABPs was conserved among different P. falciparum strains, according to sequence analysis. No HABPs were found in E-TRAMP 4. Bindings of HABPs were saturable and sensitive to the enzymatic treatment of RBCs and HABPs had different structural features, according to circular dichroism studies. Our results suggest that the REX and E-TRAMP families participate in relevant interactions with RBC membrane proteins, which highlight these proteins as potential targets for the development of fully effective immunoprophylactic methods. © 2009 Elsevier Ltd. All rights reserved.

AB - Severe malaria pathology is directly associated with cytoadherence of infected red blood cells (iRBCs) to healthy RBCs and/or endothelial cells occurring during the intraerythrocytic development of Plasmodium falciparum. We synthesized, as 20-mer long peptides, the members of the ring exported (REX) protein family encoded in chromosome 9, as well as the early transcribed membrane proteins (E-TRAMP) 10.2 and 4, to identify specific RBC binding regions in these proteins. Twelve binding peptides were identified (designated as HABPs): three were identified in REX1, two in REX2, one in REX3, two in REX4 and four in E-TRAMP 10.2. The majority of these HABPs was conserved among different P. falciparum strains, according to sequence analysis. No HABPs were found in E-TRAMP 4. Bindings of HABPs were saturable and sensitive to the enzymatic treatment of RBCs and HABPs had different structural features, according to circular dichroism studies. Our results suggest that the REX and E-TRAMP families participate in relevant interactions with RBC membrane proteins, which highlight these proteins as potential targets for the development of fully effective immunoprophylactic methods. © 2009 Elsevier Ltd. All rights reserved.

U2 - 10.1016/j.vaccine.2009.09.009

DO - 10.1016/j.vaccine.2009.09.009

M3 - Article

SP - 6877

EP - 6886

JO - Vaccine

JF - Vaccine

SN - 0264-410X

ER -