3D structure and immunogenicity of Plasmodium falciparum sporozoite induced associated protein peptides as components of fully-protective anti-malarial vaccine

Martha P. Alba, Hannia Almonacid, Dayana Calderón, Edgar A. Chacón, Luis A. Poloche, Manuel A. Patarroyo, Manuel E. Patarroyo

Resultado de la investigación: Contribución a RevistaArtículo

2 Citas (Scopus)

Resumen

SIAP-1 and SIAP-2 are proteins which are implicated in early events involving Plasmodium falciparum infection of the Anopheles mosquito vector and the human host. High affinity HeLa and HepG2 cell binding conserved peptides have been previously identified in these proteins, i.e. SIAP-1 34893 ( 421KVQGLSYLLRRKNGTKHPVY 440) and SIAP-1 34899 ( 541YVLNSKLLNSRSFDKFKWIQ 560) and SIAP-2 36879 ( 181LLLYSTNSEDNLDISFGELQ 200). When amino acid sequences have been properly modified (replacements shown in bold) they have induced high antibody titres against sporozoites in Aotus monkeys (assessed by IFA) and in the corresponding recombinant proteins (determined by ELISA and Western blot). 1H NMR studies of these conserved native and modified high activity binding peptides (HABPs) revealed that all had α-helical structures in different locations and lengths. Conserved and corresponding modified HABPs displayed different lengths between the residues fitting into MHCII molecule pockets 1-9 and different amino acid orientation based on their different HLA-DRβ1 * binding motifs and binding registers, suggesting that such modifications were associated with making them immunogenic. The results suggested that these modified HAPBs could be potential targets for inclusion as components of a fully-effective, minimal sub-unit based, multi-epitope, and multistage anti-malarial vaccine. © 2011 Elsevier Inc..
Idioma originalEnglish (US)
Páginas (desde-hasta)349-355
Número de páginas7
PublicaciónBiochemical and Biophysical Research Communications
DOI
EstadoPublished - dic 16 2011

Huella dactilar

Malaria Vaccines
Sporozoites
Antimalarials
Plasmodium falciparum
Peptides
Amino Acids
Proteins
Anopheles
Hep G2 Cells
HeLa Cells
Recombinant Proteins
Malaria
Haplorhini
Epitopes
Amino Acid Sequence
Western Blotting
Enzyme-Linked Immunosorbent Assay
Nuclear magnetic resonance
Molecules
Antibodies

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title = "3D structure and immunogenicity of Plasmodium falciparum sporozoite induced associated protein peptides as components of fully-protective anti-malarial vaccine",
abstract = "SIAP-1 and SIAP-2 are proteins which are implicated in early events involving Plasmodium falciparum infection of the Anopheles mosquito vector and the human host. High affinity HeLa and HepG2 cell binding conserved peptides have been previously identified in these proteins, i.e. SIAP-1 34893 ( 421KVQGLSYLLRRKNGTKHPVY 440) and SIAP-1 34899 ( 541YVLNSKLLNSRSFDKFKWIQ 560) and SIAP-2 36879 ( 181LLLYSTNSEDNLDISFGELQ 200). When amino acid sequences have been properly modified (replacements shown in bold) they have induced high antibody titres against sporozoites in Aotus monkeys (assessed by IFA) and in the corresponding recombinant proteins (determined by ELISA and Western blot). 1H NMR studies of these conserved native and modified high activity binding peptides (HABPs) revealed that all had α-helical structures in different locations and lengths. Conserved and corresponding modified HABPs displayed different lengths between the residues fitting into MHCII molecule pockets 1-9 and different amino acid orientation based on their different HLA-DRβ1 * binding motifs and binding registers, suggesting that such modifications were associated with making them immunogenic. The results suggested that these modified HAPBs could be potential targets for inclusion as components of a fully-effective, minimal sub-unit based, multi-epitope, and multistage anti-malarial vaccine. {\circledC} 2011 Elsevier Inc..",
author = "Alba, {Martha P.} and Hannia Almonacid and Dayana Calder{\'o}n and Chac{\'o}n, {Edgar A.} and Poloche, {Luis A.} and Patarroyo, {Manuel A.} and Patarroyo, {Manuel E.}",
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3D structure and immunogenicity of Plasmodium falciparum sporozoite induced associated protein peptides as components of fully-protective anti-malarial vaccine. / Alba, Martha P.; Almonacid, Hannia; Calderón, Dayana; Chacón, Edgar A.; Poloche, Luis A.; Patarroyo, Manuel A.; Patarroyo, Manuel E.

En: Biochemical and Biophysical Research Communications, 16.12.2011, p. 349-355.

Resultado de la investigación: Contribución a RevistaArtículo

TY - JOUR

T1 - 3D structure and immunogenicity of Plasmodium falciparum sporozoite induced associated protein peptides as components of fully-protective anti-malarial vaccine

AU - Alba, Martha P.

AU - Almonacid, Hannia

AU - Calderón, Dayana

AU - Chacón, Edgar A.

AU - Poloche, Luis A.

AU - Patarroyo, Manuel A.

AU - Patarroyo, Manuel E.

PY - 2011/12/16

Y1 - 2011/12/16

N2 - SIAP-1 and SIAP-2 are proteins which are implicated in early events involving Plasmodium falciparum infection of the Anopheles mosquito vector and the human host. High affinity HeLa and HepG2 cell binding conserved peptides have been previously identified in these proteins, i.e. SIAP-1 34893 ( 421KVQGLSYLLRRKNGTKHPVY 440) and SIAP-1 34899 ( 541YVLNSKLLNSRSFDKFKWIQ 560) and SIAP-2 36879 ( 181LLLYSTNSEDNLDISFGELQ 200). When amino acid sequences have been properly modified (replacements shown in bold) they have induced high antibody titres against sporozoites in Aotus monkeys (assessed by IFA) and in the corresponding recombinant proteins (determined by ELISA and Western blot). 1H NMR studies of these conserved native and modified high activity binding peptides (HABPs) revealed that all had α-helical structures in different locations and lengths. Conserved and corresponding modified HABPs displayed different lengths between the residues fitting into MHCII molecule pockets 1-9 and different amino acid orientation based on their different HLA-DRβ1 * binding motifs and binding registers, suggesting that such modifications were associated with making them immunogenic. The results suggested that these modified HAPBs could be potential targets for inclusion as components of a fully-effective, minimal sub-unit based, multi-epitope, and multistage anti-malarial vaccine. © 2011 Elsevier Inc..

AB - SIAP-1 and SIAP-2 are proteins which are implicated in early events involving Plasmodium falciparum infection of the Anopheles mosquito vector and the human host. High affinity HeLa and HepG2 cell binding conserved peptides have been previously identified in these proteins, i.e. SIAP-1 34893 ( 421KVQGLSYLLRRKNGTKHPVY 440) and SIAP-1 34899 ( 541YVLNSKLLNSRSFDKFKWIQ 560) and SIAP-2 36879 ( 181LLLYSTNSEDNLDISFGELQ 200). When amino acid sequences have been properly modified (replacements shown in bold) they have induced high antibody titres against sporozoites in Aotus monkeys (assessed by IFA) and in the corresponding recombinant proteins (determined by ELISA and Western blot). 1H NMR studies of these conserved native and modified high activity binding peptides (HABPs) revealed that all had α-helical structures in different locations and lengths. Conserved and corresponding modified HABPs displayed different lengths between the residues fitting into MHCII molecule pockets 1-9 and different amino acid orientation based on their different HLA-DRβ1 * binding motifs and binding registers, suggesting that such modifications were associated with making them immunogenic. The results suggested that these modified HAPBs could be potential targets for inclusion as components of a fully-effective, minimal sub-unit based, multi-epitope, and multistage anti-malarial vaccine. © 2011 Elsevier Inc..

U2 - 10.1016/j.bbrc.2011.11.039

DO - 10.1016/j.bbrc.2011.11.039

M3 - Article

SP - 349

EP - 355

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

ER -