Elongating modified conserved peptides eliminates their immunogenicity and protective efficacy against P. falciparum malaria.

Adriana Janneth Bermudez Quintero, Fabiola Espejo, Zuly J. Rivera, Elizabeth Torres, Luz Mary Salazar, Manuel Elkin Patarroyo, Magnolia Vanegas Murcia

Resultado de la investigación: Contribución a RevistaArtículo

3 Citas (Scopus)

Resumen

Plasmodium falciparum malaria protein peptides were synthesised in the search for more effective routes for inducing a protective immune response against this deadly parasite and this information has been associated with such molecules' three-dimensional structure. These peptides had high red blood cell binding activity and their carboxy- and amino-terminal extremes were elongated for determining their immunogenic and protection-inducing activity against this disease in the Aotus monkey experimental model. 1H-NMR was used for analysing their three-dimensional structure; FAST ELISA, immunofluorescence antibody test, and Western blot were used for identifying their antibody inducing capacity and these previously immunised Aotus were inoculated with a highly infective P. falciparum strain to determine whether these elongated peptides were able to induce protection. This was aimed at establishing an association or correlation between long peptides' three-dimensional structure and their immunogenic and protection-inducing response in these monkeys. Peptides 20026 (25 residue), 20028 (30 residue), and 20030 (35 residues) were synthesised based on elongating the amino-terminal region of the 10022 highly immunogenic and protection-inducing modified peptide. 1H-NMR studies revealed that the first three had Classical type III beta-turn structures, different from the 20-amino acid long modified peptide 10022 which had a distorted type III beta-turn. Humoral immune response analysis showed that even when some antibodies could be generated against the parasite, none of the immunised Aotus could be protected with elongated peptides suggesting that elongating them eliminated modified peptide 10022 immunogenic and protection-inducing capacity.
Idioma originalEnglish (US)
Páginas (desde-hasta)245-258
Número de páginas14
PublicaciónJournal of Structural Biology
Volumen150
N.º3
DOI
EstadoPublished - jun 2005

Huella dactilar

Falciparum Malaria
Peptides
Haplorhini
Antibodies
Parasites
Plasmodium falciparum
Humoral Immunity
Fluorescent Antibody Technique
Theoretical Models
Erythrocytes
Western Blotting
Enzyme-Linked Immunosorbent Assay
Amino Acids

Citar esto

Bermudez Quintero, A. J., Espejo, F., Rivera, Z. J., Torres, E., Salazar, L. M., Patarroyo, M. E., & Vanegas Murcia, M. (2005). Elongating modified conserved peptides eliminates their immunogenicity and protective efficacy against P. falciparum malaria. Journal of Structural Biology, 150(3), 245-258. https://doi.org/10.1016/j.jsb.2005.03.007
Bermudez Quintero, Adriana Janneth ; Espejo, Fabiola ; Rivera, Zuly J. ; Torres, Elizabeth ; Salazar, Luz Mary ; Patarroyo, Manuel Elkin ; Vanegas Murcia, Magnolia. / Elongating modified conserved peptides eliminates their immunogenicity and protective efficacy against P. falciparum malaria. En: Journal of Structural Biology. 2005 ; Vol. 150, N.º 3. pp. 245-258.
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title = "Elongating modified conserved peptides eliminates their immunogenicity and protective efficacy against P. falciparum malaria.",
abstract = "Plasmodium falciparum malaria protein peptides were synthesised in the search for more effective routes for inducing a protective immune response against this deadly parasite and this information has been associated with such molecules' three-dimensional structure. These peptides had high red blood cell binding activity and their carboxy- and amino-terminal extremes were elongated for determining their immunogenic and protection-inducing activity against this disease in the Aotus monkey experimental model. 1H-NMR was used for analysing their three-dimensional structure; FAST ELISA, immunofluorescence antibody test, and Western blot were used for identifying their antibody inducing capacity and these previously immunised Aotus were inoculated with a highly infective P. falciparum strain to determine whether these elongated peptides were able to induce protection. This was aimed at establishing an association or correlation between long peptides' three-dimensional structure and their immunogenic and protection-inducing response in these monkeys. Peptides 20026 (25 residue), 20028 (30 residue), and 20030 (35 residues) were synthesised based on elongating the amino-terminal region of the 10022 highly immunogenic and protection-inducing modified peptide. 1H-NMR studies revealed that the first three had Classical type III beta-turn structures, different from the 20-amino acid long modified peptide 10022 which had a distorted type III beta-turn. Humoral immune response analysis showed that even when some antibodies could be generated against the parasite, none of the immunised Aotus could be protected with elongated peptides suggesting that elongating them eliminated modified peptide 10022 immunogenic and protection-inducing capacity.",
author = "{Bermudez Quintero}, {Adriana Janneth} and Fabiola Espejo and Rivera, {Zuly J.} and Elizabeth Torres and Salazar, {Luz Mary} and Patarroyo, {Manuel Elkin} and {Vanegas Murcia}, Magnolia",
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Bermudez Quintero, AJ, Espejo, F, Rivera, ZJ, Torres, E, Salazar, LM, Patarroyo, ME & Vanegas Murcia, M 2005, 'Elongating modified conserved peptides eliminates their immunogenicity and protective efficacy against P. falciparum malaria.', Journal of Structural Biology, vol. 150, n.º 3, pp. 245-258. https://doi.org/10.1016/j.jsb.2005.03.007

Elongating modified conserved peptides eliminates their immunogenicity and protective efficacy against P. falciparum malaria. / Bermudez Quintero, Adriana Janneth; Espejo, Fabiola; Rivera, Zuly J.; Torres, Elizabeth; Salazar, Luz Mary; Patarroyo, Manuel Elkin; Vanegas Murcia, Magnolia.

En: Journal of Structural Biology, Vol. 150, N.º 3, 06.2005, p. 245-258.

Resultado de la investigación: Contribución a RevistaArtículo

TY - JOUR

T1 - Elongating modified conserved peptides eliminates their immunogenicity and protective efficacy against P. falciparum malaria.

AU - Bermudez Quintero, Adriana Janneth

AU - Espejo, Fabiola

AU - Rivera, Zuly J.

AU - Torres, Elizabeth

AU - Salazar, Luz Mary

AU - Patarroyo, Manuel Elkin

AU - Vanegas Murcia, Magnolia

PY - 2005/6

Y1 - 2005/6

N2 - Plasmodium falciparum malaria protein peptides were synthesised in the search for more effective routes for inducing a protective immune response against this deadly parasite and this information has been associated with such molecules' three-dimensional structure. These peptides had high red blood cell binding activity and their carboxy- and amino-terminal extremes were elongated for determining their immunogenic and protection-inducing activity against this disease in the Aotus monkey experimental model. 1H-NMR was used for analysing their three-dimensional structure; FAST ELISA, immunofluorescence antibody test, and Western blot were used for identifying their antibody inducing capacity and these previously immunised Aotus were inoculated with a highly infective P. falciparum strain to determine whether these elongated peptides were able to induce protection. This was aimed at establishing an association or correlation between long peptides' three-dimensional structure and their immunogenic and protection-inducing response in these monkeys. Peptides 20026 (25 residue), 20028 (30 residue), and 20030 (35 residues) were synthesised based on elongating the amino-terminal region of the 10022 highly immunogenic and protection-inducing modified peptide. 1H-NMR studies revealed that the first three had Classical type III beta-turn structures, different from the 20-amino acid long modified peptide 10022 which had a distorted type III beta-turn. Humoral immune response analysis showed that even when some antibodies could be generated against the parasite, none of the immunised Aotus could be protected with elongated peptides suggesting that elongating them eliminated modified peptide 10022 immunogenic and protection-inducing capacity.

AB - Plasmodium falciparum malaria protein peptides were synthesised in the search for more effective routes for inducing a protective immune response against this deadly parasite and this information has been associated with such molecules' three-dimensional structure. These peptides had high red blood cell binding activity and their carboxy- and amino-terminal extremes were elongated for determining their immunogenic and protection-inducing activity against this disease in the Aotus monkey experimental model. 1H-NMR was used for analysing their three-dimensional structure; FAST ELISA, immunofluorescence antibody test, and Western blot were used for identifying their antibody inducing capacity and these previously immunised Aotus were inoculated with a highly infective P. falciparum strain to determine whether these elongated peptides were able to induce protection. This was aimed at establishing an association or correlation between long peptides' three-dimensional structure and their immunogenic and protection-inducing response in these monkeys. Peptides 20026 (25 residue), 20028 (30 residue), and 20030 (35 residues) were synthesised based on elongating the amino-terminal region of the 10022 highly immunogenic and protection-inducing modified peptide. 1H-NMR studies revealed that the first three had Classical type III beta-turn structures, different from the 20-amino acid long modified peptide 10022 which had a distorted type III beta-turn. Humoral immune response analysis showed that even when some antibodies could be generated against the parasite, none of the immunised Aotus could be protected with elongated peptides suggesting that elongating them eliminated modified peptide 10022 immunogenic and protection-inducing capacity.

UR - http://www.sciencedirect.com/science/article/pii/S1047847705000766?via%3Dihub

U2 - 10.1016/j.jsb.2005.03.007

DO - 10.1016/j.jsb.2005.03.007

M3 - Article

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SP - 245

EP - 258

JO - Journal of Structural Biology

JF - Journal of Structural Biology

SN - 1047-8477

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