Fine mapping of Plasmodium falciparum ribosomal phosphoprotein PfP0 revealed sequences with highly specific binding activity to human red blood cells

Gabriela Arevalo-Pinzon, Hernando Curtidor, Claudia Reyes, Martha Pinto, Carolina Vizcaíno, Manuel A. Patarroyo, Manuel E. Patarroyo

Resultado de la investigación: Contribución a RevistaArtículo

3 Citas (Scopus)

Resumen

The Plasmodium falciparum P0 ribosomal phosphoprotein (PfP0) was identified for the first time by screening a cDNA expression library of P. falciparum parasites with sera from malaria-immune individuals. Due to its localization on the surface of different parasite life-cycle stages (merozoites and gametocytes) and its recognition by invasion-blocking antibodies, PfP0 has been considered a potential malaria-vaccine component. In this study, 16 20-mer-long synthetic peptides spanning the entire PfP0 sequence were evaluated by means of receptor-ligand assays with human red blood cells (RBCs) in order to determine the role played by these peptides in the invasion process. Four RBC high-activity binding peptides (HABPs), located mostly toward the N-terminal region, were identified: HABP 33898 (1MAKLSKQQKKQMYIEKLSSL 20), HABP 33900 (41ASVRKSLRGKATILMGKNTRY60), HABP 33901 (61IRTALKKNLQAVPQIEKLLPY 80), and HABP 33906 (161LIKQGEKVTASSATLLRKFNY180). The binding pattern of HABPs 33898 and 33906 to enzyme-treated RBCs suggests receptors of protein nature for these two HABPs, one of which could correspond to a common 58-kDa RBC membrane protein, as indicated by results of cross-linking assays. Both HABPs exhibited high content of α-helical features and prevented P. falciparum merozoite invasion to RBCs in vitro by up to 91%. The invasion-blocking ability reported here for these PfP0 HABPs supports their inclusion in immunological studies with the aim of assessing their potential as candidates for a vaccine against P. falciparum malaria. © 2009 Springer-Verlag.
Idioma originalEnglish (US)
Páginas (desde-hasta)61-74
Número de páginas14
PublicaciónJournal of Molecular Medicine
DOI
EstadoPublished - ene 1 2010

Huella dactilar

Phosphoproteins
Plasmodium falciparum
Human Activities
Erythrocytes
Peptides
Merozoites
Parasites
Malaria Vaccines
Blocking Antibodies
Falciparum Malaria
Life Cycle Stages
Gene Library
Malaria
Immune Sera
Membrane Proteins
Vaccines
Ligands

Citar esto

Arevalo-Pinzon, Gabriela ; Curtidor, Hernando ; Reyes, Claudia ; Pinto, Martha ; Vizcaíno, Carolina ; Patarroyo, Manuel A. ; Patarroyo, Manuel E. / Fine mapping of Plasmodium falciparum ribosomal phosphoprotein PfP0 revealed sequences with highly specific binding activity to human red blood cells. En: Journal of Molecular Medicine. 2010 ; pp. 61-74.
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title = "Fine mapping of Plasmodium falciparum ribosomal phosphoprotein PfP0 revealed sequences with highly specific binding activity to human red blood cells",
abstract = "The Plasmodium falciparum P0 ribosomal phosphoprotein (PfP0) was identified for the first time by screening a cDNA expression library of P. falciparum parasites with sera from malaria-immune individuals. Due to its localization on the surface of different parasite life-cycle stages (merozoites and gametocytes) and its recognition by invasion-blocking antibodies, PfP0 has been considered a potential malaria-vaccine component. In this study, 16 20-mer-long synthetic peptides spanning the entire PfP0 sequence were evaluated by means of receptor-ligand assays with human red blood cells (RBCs) in order to determine the role played by these peptides in the invasion process. Four RBC high-activity binding peptides (HABPs), located mostly toward the N-terminal region, were identified: HABP 33898 (1MAKLSKQQKKQMYIEKLSSL 20), HABP 33900 (41ASVRKSLRGKATILMGKNTRY60), HABP 33901 (61IRTALKKNLQAVPQIEKLLPY 80), and HABP 33906 (161LIKQGEKVTASSATLLRKFNY180). The binding pattern of HABPs 33898 and 33906 to enzyme-treated RBCs suggests receptors of protein nature for these two HABPs, one of which could correspond to a common 58-kDa RBC membrane protein, as indicated by results of cross-linking assays. Both HABPs exhibited high content of α-helical features and prevented P. falciparum merozoite invasion to RBCs in vitro by up to 91{\%}. The invasion-blocking ability reported here for these PfP0 HABPs supports their inclusion in immunological studies with the aim of assessing their potential as candidates for a vaccine against P. falciparum malaria. {\circledC} 2009 Springer-Verlag.",
author = "Gabriela Arevalo-Pinzon and Hernando Curtidor and Claudia Reyes and Martha Pinto and Carolina Vizca{\'i}no and Patarroyo, {Manuel A.} and Patarroyo, {Manuel E.}",
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doi = "10.1007/s00109-009-0533-5",
language = "English (US)",
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Fine mapping of Plasmodium falciparum ribosomal phosphoprotein PfP0 revealed sequences with highly specific binding activity to human red blood cells. / Arevalo-Pinzon, Gabriela; Curtidor, Hernando; Reyes, Claudia; Pinto, Martha; Vizcaíno, Carolina; Patarroyo, Manuel A.; Patarroyo, Manuel E.

En: Journal of Molecular Medicine, 01.01.2010, p. 61-74.

Resultado de la investigación: Contribución a RevistaArtículo

TY - JOUR

T1 - Fine mapping of Plasmodium falciparum ribosomal phosphoprotein PfP0 revealed sequences with highly specific binding activity to human red blood cells

AU - Arevalo-Pinzon, Gabriela

AU - Curtidor, Hernando

AU - Reyes, Claudia

AU - Pinto, Martha

AU - Vizcaíno, Carolina

AU - Patarroyo, Manuel A.

AU - Patarroyo, Manuel E.

PY - 2010/1/1

Y1 - 2010/1/1

N2 - The Plasmodium falciparum P0 ribosomal phosphoprotein (PfP0) was identified for the first time by screening a cDNA expression library of P. falciparum parasites with sera from malaria-immune individuals. Due to its localization on the surface of different parasite life-cycle stages (merozoites and gametocytes) and its recognition by invasion-blocking antibodies, PfP0 has been considered a potential malaria-vaccine component. In this study, 16 20-mer-long synthetic peptides spanning the entire PfP0 sequence were evaluated by means of receptor-ligand assays with human red blood cells (RBCs) in order to determine the role played by these peptides in the invasion process. Four RBC high-activity binding peptides (HABPs), located mostly toward the N-terminal region, were identified: HABP 33898 (1MAKLSKQQKKQMYIEKLSSL 20), HABP 33900 (41ASVRKSLRGKATILMGKNTRY60), HABP 33901 (61IRTALKKNLQAVPQIEKLLPY 80), and HABP 33906 (161LIKQGEKVTASSATLLRKFNY180). The binding pattern of HABPs 33898 and 33906 to enzyme-treated RBCs suggests receptors of protein nature for these two HABPs, one of which could correspond to a common 58-kDa RBC membrane protein, as indicated by results of cross-linking assays. Both HABPs exhibited high content of α-helical features and prevented P. falciparum merozoite invasion to RBCs in vitro by up to 91%. The invasion-blocking ability reported here for these PfP0 HABPs supports their inclusion in immunological studies with the aim of assessing their potential as candidates for a vaccine against P. falciparum malaria. © 2009 Springer-Verlag.

AB - The Plasmodium falciparum P0 ribosomal phosphoprotein (PfP0) was identified for the first time by screening a cDNA expression library of P. falciparum parasites with sera from malaria-immune individuals. Due to its localization on the surface of different parasite life-cycle stages (merozoites and gametocytes) and its recognition by invasion-blocking antibodies, PfP0 has been considered a potential malaria-vaccine component. In this study, 16 20-mer-long synthetic peptides spanning the entire PfP0 sequence were evaluated by means of receptor-ligand assays with human red blood cells (RBCs) in order to determine the role played by these peptides in the invasion process. Four RBC high-activity binding peptides (HABPs), located mostly toward the N-terminal region, were identified: HABP 33898 (1MAKLSKQQKKQMYIEKLSSL 20), HABP 33900 (41ASVRKSLRGKATILMGKNTRY60), HABP 33901 (61IRTALKKNLQAVPQIEKLLPY 80), and HABP 33906 (161LIKQGEKVTASSATLLRKFNY180). The binding pattern of HABPs 33898 and 33906 to enzyme-treated RBCs suggests receptors of protein nature for these two HABPs, one of which could correspond to a common 58-kDa RBC membrane protein, as indicated by results of cross-linking assays. Both HABPs exhibited high content of α-helical features and prevented P. falciparum merozoite invasion to RBCs in vitro by up to 91%. The invasion-blocking ability reported here for these PfP0 HABPs supports their inclusion in immunological studies with the aim of assessing their potential as candidates for a vaccine against P. falciparum malaria. © 2009 Springer-Verlag.

U2 - 10.1007/s00109-009-0533-5

DO - 10.1007/s00109-009-0533-5

M3 - Article

SP - 61

EP - 74

JO - Journal of Molecular Medicine

JF - Journal of Molecular Medicine

SN - 0946-2716

ER -