Binding activity, structure, and immunogenicity of synthetic peptides derived from Plasmodium falciparum CelTOS and TRSP proteins

Hernando Curtidor, Gabriela Arévalo-Pinzón, Adriana Bermudez, Dayana Calderon, Magnolia Vanegas, Liliana C. Patiño, Manuel A. Patarroyo, Manuel E. Patarroyo

Resultado de la investigación: Contribución a RevistaArtículo

4 Citas (Scopus)

Resumen

Several sporozoite proteins have been associated with Plasmodium falciparum cell traversal and hepatocyte invasion, including the cell-traversal protein for ookinetes and sporozoites (CelTOS), and thrombospondin-related sporozoite protein (TRSP). CelTOS and TRSP amino acid sequences have been finely mapped to identify regions specifically binding to HeLa and HepG2 cells, respectively. Three high-activity binding peptides (HABPs) were found in CelTOS and one HABP was found in TRSP, all of them having high α-helical structure content. These HABPs' specific binding was sensitive to HeLa and HepG2 cells' pre-treatment with heparinase I and chondroitinase ABC. Despite their similarity at three-dimensional (3D) structural level, TRSP and TRAP HABPs located in the TSR domain did not compete for the same binding sites. CelTOS and TRSP HABPs were used as a template for designing modified sequences to then be assessed in the Aotus monkey experimental model. Antibodies directed against these modified HABPs were able to recognize both the native parasite protein by immunofluorescence assay and the recombinant protein (expressed in Escherichia coli) by Western blot and ELISA assays. The results suggested that these modified HABPs could be promising targets in designing a fully effective, antimalarial vaccine. © 2011 Springer-Verlag.
Idioma originalEnglish (US)
Páginas (desde-hasta)365-378
Número de páginas14
PublicaciónAmino Acids
DOI
EstadoPublished - jul 1 2012

Huella dactilar

Thrombospondins
Sporozoites
Plasmodium falciparum
Peptides
Proteins
Hep G2 Cells
HeLa Cells
Assays
Heparin Lyase
Chondroitin ABC Lyase
Antimalarials
Recombinant Proteins
Escherichia coli
Haplorhini
Fluorescent Antibody Technique
Hepatocytes
Amino Acid Sequence
Parasites
Theoretical Models
Vaccines

Citar esto

Curtidor, H., Arévalo-Pinzón, G., Bermudez, A., Calderon, D., Vanegas, M., Patiño, L. C., ... Patarroyo, M. E. (2012). Binding activity, structure, and immunogenicity of synthetic peptides derived from Plasmodium falciparum CelTOS and TRSP proteins. Amino Acids, 365-378. https://doi.org/10.1007/s00726-011-1087-8
Curtidor, Hernando ; Arévalo-Pinzón, Gabriela ; Bermudez, Adriana ; Calderon, Dayana ; Vanegas, Magnolia ; Patiño, Liliana C. ; Patarroyo, Manuel A. ; Patarroyo, Manuel E. / Binding activity, structure, and immunogenicity of synthetic peptides derived from Plasmodium falciparum CelTOS and TRSP proteins. En: Amino Acids. 2012 ; pp. 365-378.
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abstract = "Several sporozoite proteins have been associated with Plasmodium falciparum cell traversal and hepatocyte invasion, including the cell-traversal protein for ookinetes and sporozoites (CelTOS), and thrombospondin-related sporozoite protein (TRSP). CelTOS and TRSP amino acid sequences have been finely mapped to identify regions specifically binding to HeLa and HepG2 cells, respectively. Three high-activity binding peptides (HABPs) were found in CelTOS and one HABP was found in TRSP, all of them having high α-helical structure content. These HABPs' specific binding was sensitive to HeLa and HepG2 cells' pre-treatment with heparinase I and chondroitinase ABC. Despite their similarity at three-dimensional (3D) structural level, TRSP and TRAP HABPs located in the TSR domain did not compete for the same binding sites. CelTOS and TRSP HABPs were used as a template for designing modified sequences to then be assessed in the Aotus monkey experimental model. Antibodies directed against these modified HABPs were able to recognize both the native parasite protein by immunofluorescence assay and the recombinant protein (expressed in Escherichia coli) by Western blot and ELISA assays. The results suggested that these modified HABPs could be promising targets in designing a fully effective, antimalarial vaccine. {\circledC} 2011 Springer-Verlag.",
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Binding activity, structure, and immunogenicity of synthetic peptides derived from Plasmodium falciparum CelTOS and TRSP proteins. / Curtidor, Hernando; Arévalo-Pinzón, Gabriela; Bermudez, Adriana; Calderon, Dayana; Vanegas, Magnolia; Patiño, Liliana C.; Patarroyo, Manuel A.; Patarroyo, Manuel E.

En: Amino Acids, 01.07.2012, p. 365-378.

Resultado de la investigación: Contribución a RevistaArtículo

TY - JOUR

T1 - Binding activity, structure, and immunogenicity of synthetic peptides derived from Plasmodium falciparum CelTOS and TRSP proteins

AU - Curtidor, Hernando

AU - Arévalo-Pinzón, Gabriela

AU - Bermudez, Adriana

AU - Calderon, Dayana

AU - Vanegas, Magnolia

AU - Patiño, Liliana C.

AU - Patarroyo, Manuel A.

AU - Patarroyo, Manuel E.

PY - 2012/7/1

Y1 - 2012/7/1

N2 - Several sporozoite proteins have been associated with Plasmodium falciparum cell traversal and hepatocyte invasion, including the cell-traversal protein for ookinetes and sporozoites (CelTOS), and thrombospondin-related sporozoite protein (TRSP). CelTOS and TRSP amino acid sequences have been finely mapped to identify regions specifically binding to HeLa and HepG2 cells, respectively. Three high-activity binding peptides (HABPs) were found in CelTOS and one HABP was found in TRSP, all of them having high α-helical structure content. These HABPs' specific binding was sensitive to HeLa and HepG2 cells' pre-treatment with heparinase I and chondroitinase ABC. Despite their similarity at three-dimensional (3D) structural level, TRSP and TRAP HABPs located in the TSR domain did not compete for the same binding sites. CelTOS and TRSP HABPs were used as a template for designing modified sequences to then be assessed in the Aotus monkey experimental model. Antibodies directed against these modified HABPs were able to recognize both the native parasite protein by immunofluorescence assay and the recombinant protein (expressed in Escherichia coli) by Western blot and ELISA assays. The results suggested that these modified HABPs could be promising targets in designing a fully effective, antimalarial vaccine. © 2011 Springer-Verlag.

AB - Several sporozoite proteins have been associated with Plasmodium falciparum cell traversal and hepatocyte invasion, including the cell-traversal protein for ookinetes and sporozoites (CelTOS), and thrombospondin-related sporozoite protein (TRSP). CelTOS and TRSP amino acid sequences have been finely mapped to identify regions specifically binding to HeLa and HepG2 cells, respectively. Three high-activity binding peptides (HABPs) were found in CelTOS and one HABP was found in TRSP, all of them having high α-helical structure content. These HABPs' specific binding was sensitive to HeLa and HepG2 cells' pre-treatment with heparinase I and chondroitinase ABC. Despite their similarity at three-dimensional (3D) structural level, TRSP and TRAP HABPs located in the TSR domain did not compete for the same binding sites. CelTOS and TRSP HABPs were used as a template for designing modified sequences to then be assessed in the Aotus monkey experimental model. Antibodies directed against these modified HABPs were able to recognize both the native parasite protein by immunofluorescence assay and the recombinant protein (expressed in Escherichia coli) by Western blot and ELISA assays. The results suggested that these modified HABPs could be promising targets in designing a fully effective, antimalarial vaccine. © 2011 Springer-Verlag.

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DO - 10.1007/s00726-011-1087-8

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JO - Amino Acids

JF - Amino Acids

SN - 0939-4451

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