Conserved regions from Plasmodium falciparum MSP11 specifically interact with host cells and have a potential role during merozoite invasion of red blood cells

Ana Zuleima Obando-Martinez, Hernando Curtidor, Magnolia Vanegas, Gabriela Arévalo-Pinzón, Manuel Alfonso Patarroyo, Manuel Elkin Patarroyo

Resultado de la investigación: Contribución a una revistaArtículo

2 Citas (Scopus)

Resumen

Despite significant global efforts, a completely effective vaccine against Plasmodium falciparum, the species responsible for the most serious form of malaria, has not been yet obtained. One of the most promising approaches consists in combining chemically synthesized minimal subunits of parasite proteins involved in host cell invasion, which has led to the identification of peptides with high binding activity (named HABPs) to hepatocyte and red blood cell (RBC) surface receptors in a large number of sporozoite and merozoite proteins, respectively. Among these proteins is the merozoite surface protein 11 (MSP11), which shares important structural and immunological features with the antimalarial vaccine candidates MSP1, MSP3, and MSP6. In this study, 20-mer-long synthetic peptides spanning the complete sequence of MSP11 were assessed for their ability to bind specifically to RBCs. Two HABPs with high ability to inhibit invasion of RBCs in vitro were identified (namely HABPs 33595 and 33606). HABP-RBC bindings were characterized by means of saturation assays and Hill analysis, finding cooperative interactions of high affinity for both HABPs (nH of 1.5 and 1.2, Kd of 800 and 600nM for HABPs 33595 and 33606, respectively). The nature of the possible RBC receptors for MSP11 HABPs was studied in binding assays to enzyme-treated RBCs and cross-linking assays, finding that both HABPs use mainly a sialic acid-dependent receptor. An analysis of the immunological, structural and polymorphic characteristics of MSP11 HABPs supports including these peptides in further studies with the aim of designing a fully effective protection-inducing vaccine against malaria. © 2010 Wiley-Liss, Inc.
Idioma originalInglés estadounidense
Páginas (desde-hasta)882-892
Número de páginas11
PublicaciónJournal of Cellular Biochemistry
DOI
EstadoPublicada - jul 1 2010

Huella dactilar

Merozoites
Plasmodium falciparum
Membrane Proteins
Blood
Erythrocytes
Cells
Assays
Vaccines
Peptides
Merozoite Surface Protein 1
Proteins
Antimalarials
Cell Surface Receptors
Malaria Vaccines
N-Acetylneuraminic Acid
Sporozoites
Protein Subunits
Enzyme Assays
Malaria
Hepatocytes

Citar esto

Obando-Martinez, Ana Zuleima ; Curtidor, Hernando ; Vanegas, Magnolia ; Arévalo-Pinzón, Gabriela ; Patarroyo, Manuel Alfonso ; Patarroyo, Manuel Elkin. / Conserved regions from Plasmodium falciparum MSP11 specifically interact with host cells and have a potential role during merozoite invasion of red blood cells. En: Journal of Cellular Biochemistry. 2010 ; pp. 882-892.
@article{3248c57aebe1465888c532a50cf3b15f,
title = "Conserved regions from Plasmodium falciparum MSP11 specifically interact with host cells and have a potential role during merozoite invasion of red blood cells",
abstract = "Despite significant global efforts, a completely effective vaccine against Plasmodium falciparum, the species responsible for the most serious form of malaria, has not been yet obtained. One of the most promising approaches consists in combining chemically synthesized minimal subunits of parasite proteins involved in host cell invasion, which has led to the identification of peptides with high binding activity (named HABPs) to hepatocyte and red blood cell (RBC) surface receptors in a large number of sporozoite and merozoite proteins, respectively. Among these proteins is the merozoite surface protein 11 (MSP11), which shares important structural and immunological features with the antimalarial vaccine candidates MSP1, MSP3, and MSP6. In this study, 20-mer-long synthetic peptides spanning the complete sequence of MSP11 were assessed for their ability to bind specifically to RBCs. Two HABPs with high ability to inhibit invasion of RBCs in vitro were identified (namely HABPs 33595 and 33606). HABP-RBC bindings were characterized by means of saturation assays and Hill analysis, finding cooperative interactions of high affinity for both HABPs (nH of 1.5 and 1.2, Kd of 800 and 600nM for HABPs 33595 and 33606, respectively). The nature of the possible RBC receptors for MSP11 HABPs was studied in binding assays to enzyme-treated RBCs and cross-linking assays, finding that both HABPs use mainly a sialic acid-dependent receptor. An analysis of the immunological, structural and polymorphic characteristics of MSP11 HABPs supports including these peptides in further studies with the aim of designing a fully effective protection-inducing vaccine against malaria. {\circledC} 2010 Wiley-Liss, Inc.",
author = "Obando-Martinez, {Ana Zuleima} and Hernando Curtidor and Magnolia Vanegas and Gabriela Ar{\'e}valo-Pinz{\'o}n and Patarroyo, {Manuel Alfonso} and Patarroyo, {Manuel Elkin}",
year = "2010",
month = "7",
day = "1",
doi = "10.1002/jcb.22600",
language = "English (US)",
pages = "882--892",
journal = "Journal of Cellular Biochemistry",
issn = "0730-2312",
publisher = "Wiley-Liss Inc.",

}

Conserved regions from Plasmodium falciparum MSP11 specifically interact with host cells and have a potential role during merozoite invasion of red blood cells. / Obando-Martinez, Ana Zuleima; Curtidor, Hernando; Vanegas, Magnolia; Arévalo-Pinzón, Gabriela; Patarroyo, Manuel Alfonso; Patarroyo, Manuel Elkin.

En: Journal of Cellular Biochemistry, 01.07.2010, p. 882-892.

Resultado de la investigación: Contribución a una revistaArtículo

TY - JOUR

T1 - Conserved regions from Plasmodium falciparum MSP11 specifically interact with host cells and have a potential role during merozoite invasion of red blood cells

AU - Obando-Martinez, Ana Zuleima

AU - Curtidor, Hernando

AU - Vanegas, Magnolia

AU - Arévalo-Pinzón, Gabriela

AU - Patarroyo, Manuel Alfonso

AU - Patarroyo, Manuel Elkin

PY - 2010/7/1

Y1 - 2010/7/1

N2 - Despite significant global efforts, a completely effective vaccine against Plasmodium falciparum, the species responsible for the most serious form of malaria, has not been yet obtained. One of the most promising approaches consists in combining chemically synthesized minimal subunits of parasite proteins involved in host cell invasion, which has led to the identification of peptides with high binding activity (named HABPs) to hepatocyte and red blood cell (RBC) surface receptors in a large number of sporozoite and merozoite proteins, respectively. Among these proteins is the merozoite surface protein 11 (MSP11), which shares important structural and immunological features with the antimalarial vaccine candidates MSP1, MSP3, and MSP6. In this study, 20-mer-long synthetic peptides spanning the complete sequence of MSP11 were assessed for their ability to bind specifically to RBCs. Two HABPs with high ability to inhibit invasion of RBCs in vitro were identified (namely HABPs 33595 and 33606). HABP-RBC bindings were characterized by means of saturation assays and Hill analysis, finding cooperative interactions of high affinity for both HABPs (nH of 1.5 and 1.2, Kd of 800 and 600nM for HABPs 33595 and 33606, respectively). The nature of the possible RBC receptors for MSP11 HABPs was studied in binding assays to enzyme-treated RBCs and cross-linking assays, finding that both HABPs use mainly a sialic acid-dependent receptor. An analysis of the immunological, structural and polymorphic characteristics of MSP11 HABPs supports including these peptides in further studies with the aim of designing a fully effective protection-inducing vaccine against malaria. © 2010 Wiley-Liss, Inc.

AB - Despite significant global efforts, a completely effective vaccine against Plasmodium falciparum, the species responsible for the most serious form of malaria, has not been yet obtained. One of the most promising approaches consists in combining chemically synthesized minimal subunits of parasite proteins involved in host cell invasion, which has led to the identification of peptides with high binding activity (named HABPs) to hepatocyte and red blood cell (RBC) surface receptors in a large number of sporozoite and merozoite proteins, respectively. Among these proteins is the merozoite surface protein 11 (MSP11), which shares important structural and immunological features with the antimalarial vaccine candidates MSP1, MSP3, and MSP6. In this study, 20-mer-long synthetic peptides spanning the complete sequence of MSP11 were assessed for their ability to bind specifically to RBCs. Two HABPs with high ability to inhibit invasion of RBCs in vitro were identified (namely HABPs 33595 and 33606). HABP-RBC bindings were characterized by means of saturation assays and Hill analysis, finding cooperative interactions of high affinity for both HABPs (nH of 1.5 and 1.2, Kd of 800 and 600nM for HABPs 33595 and 33606, respectively). The nature of the possible RBC receptors for MSP11 HABPs was studied in binding assays to enzyme-treated RBCs and cross-linking assays, finding that both HABPs use mainly a sialic acid-dependent receptor. An analysis of the immunological, structural and polymorphic characteristics of MSP11 HABPs supports including these peptides in further studies with the aim of designing a fully effective protection-inducing vaccine against malaria. © 2010 Wiley-Liss, Inc.

U2 - 10.1002/jcb.22600

DO - 10.1002/jcb.22600

M3 - Article

C2 - 20564187

SP - 882

EP - 892

JO - Journal of Cellular Biochemistry

JF - Journal of Cellular Biochemistry

SN - 0730-2312

ER -