Fitting modified HRP-I peptide analogue 3D structure into HLA-DR molecules induces protection against Plasmodium falciparum malaria

Adriana Janneth Bermudez Quintero, Martha Patricia Alba, Fabiola Espejo, Luis Eduardo Vargas, Claudia Parra, Raul Rodriguez, Claudia Reyes, Manuel Elkin Patarroyo

Resultado de la investigación: Contribución a RevistaArtículo

7 Citas (Scopus)

Resumen

Conserved, high-activity, red blood cell binding malaria peptide 6786, from the HRP-I protein, having a random 3D structure as determined by 1H-NMR, was non-immunogenic and non-protection inducing when used as an immunogen in Aotus monkeys. Modifications made in its amino acid sequence were thus performed to render it immunogenic and protection inducing. Non-immunogenic, non-protection inducing modified peptide 13852 presented A2-H8 and K14-L18 helix fragments. Immunogenic, non-protection inducing modified peptide 23428 presented a short, displaced helix in a different region, whilst immunogenic, protection inducing peptide 24224 had 2 displaced helical regions towards the central region giving more flexibility to its N- and C-terminals. Immunogenic and protection inducing peptides bound with high affinity to HLA-DRB1* 0301 whilst others did not bind to any HLA-DRB1* purified molecule. Structural modifications may thus lead to inducing immunogenicity and protection associated with their capacity to bind specifically to purified HLA-DRB1* molecules, suggesting a new way of developing multi-component, subunit-based malarial vaccines.
Idioma originalEnglish (US)
Páginas (desde-hasta)336-349
Número de páginas14
PublicaciónInternational Journal of Biochemistry and Cell Biology
Volumen37
N.º2
DOI
EstadoPublished - feb 2005

Huella dactilar

Falciparum Malaria
HLA-DR Antigens
Peptides
Molecules
HLA-DRB1 Chains
Malaria Vaccines
varespladib methyl
Malaria
Haplorhini
Amino Acid Sequence
Blood
Erythrocytes
Cells
Nuclear magnetic resonance
Amino Acids
Proteins

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Bermudez Quintero, Adriana Janneth ; Alba, Martha Patricia ; Espejo, Fabiola ; Vargas, Luis Eduardo ; Parra, Claudia ; Rodriguez, Raul ; Reyes, Claudia ; Patarroyo, Manuel Elkin. / Fitting modified HRP-I peptide analogue 3D structure into HLA-DR molecules induces protection against Plasmodium falciparum malaria. En: International Journal of Biochemistry and Cell Biology. 2005 ; Vol. 37, N.º 2. pp. 336-349.
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title = "Fitting modified HRP-I peptide analogue 3D structure into HLA-DR molecules induces protection against Plasmodium falciparum malaria",
abstract = "Conserved, high-activity, red blood cell binding malaria peptide 6786, from the HRP-I protein, having a random 3D structure as determined by 1H-NMR, was non-immunogenic and non-protection inducing when used as an immunogen in Aotus monkeys. Modifications made in its amino acid sequence were thus performed to render it immunogenic and protection inducing. Non-immunogenic, non-protection inducing modified peptide 13852 presented A2-H8 and K14-L18 helix fragments. Immunogenic, non-protection inducing modified peptide 23428 presented a short, displaced helix in a different region, whilst immunogenic, protection inducing peptide 24224 had 2 displaced helical regions towards the central region giving more flexibility to its N- and C-terminals. Immunogenic and protection inducing peptides bound with high affinity to HLA-DRB1* 0301 whilst others did not bind to any HLA-DRB1* purified molecule. Structural modifications may thus lead to inducing immunogenicity and protection associated with their capacity to bind specifically to purified HLA-DRB1* molecules, suggesting a new way of developing multi-component, subunit-based malarial vaccines.",
author = "{Bermudez Quintero}, {Adriana Janneth} and Alba, {Martha Patricia} and Fabiola Espejo and Vargas, {Luis Eduardo} and Claudia Parra and Raul Rodriguez and Claudia Reyes and Patarroyo, {Manuel Elkin}",
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Fitting modified HRP-I peptide analogue 3D structure into HLA-DR molecules induces protection against Plasmodium falciparum malaria. / Bermudez Quintero, Adriana Janneth; Alba, Martha Patricia; Espejo, Fabiola; Vargas, Luis Eduardo; Parra, Claudia ; Rodriguez, Raul; Reyes, Claudia; Patarroyo, Manuel Elkin.

En: International Journal of Biochemistry and Cell Biology, Vol. 37, N.º 2, 02.2005, p. 336-349.

Resultado de la investigación: Contribución a RevistaArtículo

TY - JOUR

T1 - Fitting modified HRP-I peptide analogue 3D structure into HLA-DR molecules induces protection against Plasmodium falciparum malaria

AU - Bermudez Quintero, Adriana Janneth

AU - Alba, Martha Patricia

AU - Espejo, Fabiola

AU - Vargas, Luis Eduardo

AU - Parra, Claudia

AU - Rodriguez, Raul

AU - Reyes, Claudia

AU - Patarroyo, Manuel Elkin

PY - 2005/2

Y1 - 2005/2

N2 - Conserved, high-activity, red blood cell binding malaria peptide 6786, from the HRP-I protein, having a random 3D structure as determined by 1H-NMR, was non-immunogenic and non-protection inducing when used as an immunogen in Aotus monkeys. Modifications made in its amino acid sequence were thus performed to render it immunogenic and protection inducing. Non-immunogenic, non-protection inducing modified peptide 13852 presented A2-H8 and K14-L18 helix fragments. Immunogenic, non-protection inducing modified peptide 23428 presented a short, displaced helix in a different region, whilst immunogenic, protection inducing peptide 24224 had 2 displaced helical regions towards the central region giving more flexibility to its N- and C-terminals. Immunogenic and protection inducing peptides bound with high affinity to HLA-DRB1* 0301 whilst others did not bind to any HLA-DRB1* purified molecule. Structural modifications may thus lead to inducing immunogenicity and protection associated with their capacity to bind specifically to purified HLA-DRB1* molecules, suggesting a new way of developing multi-component, subunit-based malarial vaccines.

AB - Conserved, high-activity, red blood cell binding malaria peptide 6786, from the HRP-I protein, having a random 3D structure as determined by 1H-NMR, was non-immunogenic and non-protection inducing when used as an immunogen in Aotus monkeys. Modifications made in its amino acid sequence were thus performed to render it immunogenic and protection inducing. Non-immunogenic, non-protection inducing modified peptide 13852 presented A2-H8 and K14-L18 helix fragments. Immunogenic, non-protection inducing modified peptide 23428 presented a short, displaced helix in a different region, whilst immunogenic, protection inducing peptide 24224 had 2 displaced helical regions towards the central region giving more flexibility to its N- and C-terminals. Immunogenic and protection inducing peptides bound with high affinity to HLA-DRB1* 0301 whilst others did not bind to any HLA-DRB1* purified molecule. Structural modifications may thus lead to inducing immunogenicity and protection associated with their capacity to bind specifically to purified HLA-DRB1* molecules, suggesting a new way of developing multi-component, subunit-based malarial vaccines.

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U2 - 10.1016/j.biocel.2004.07.012

DO - 10.1016/j.biocel.2004.07.012

M3 - Article

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SP - 336

EP - 349

JO - International Journal of Biochemistry and Cell Biology

JF - International Journal of Biochemistry and Cell Biology

SN - 1357-2725

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