The GPI-anchored 6-Cys Protein Pv12 is Present in Detergent-resistant Microdomains of Plasmodium vivax Blood Stage Schizonts

Plasmodium vivax malaria remains one of the tropical diseases causing an enormous burden on global public health. Several proteins located on this parasite species' merozoite surface have been considered the most suitable antigens for being included in an anti-malarial vaccine, given the functi...

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Autores:
Tipo de recurso:
Fecha de publicación:
2013
Institución:
Universidad del Rosario
Repositorio:
Repositorio EdocUR - U. Rosario
Idioma:
eng
OAI Identifier:
oai:repository.urosario.edu.co:10336/22896
Acceso en línea:
https://doi.org/10.1016/j.protis.2012.03.001
https://repository.urosario.edu.co/handle/10336/22896
Palabra clave:
Parasite antigen
Protozoal dna
Protozoal protein
Amino acid sequence
Animal
Article
Cell membrane
Chemistry
Dna sequence
Erythrocyte
Genetics
Haplorhini
Isolation and purification
Molecular genetics
Nucleotide sequence
Parasitology
Plasmodium vivax
Protein tertiary structure
Schizont
Sequence alignment
Amino acid sequence
Animals
Erythrocytes
Haplorhini
Membrane microdomains
Molecular sequence data
Plasmodium vivax
Protozoan proteins
Schizonts
Sequence alignment
Plasmodium vivax
6-cys domain
Antigen
Detergent-resistant membrane
Glycosylphosphatidylinositol-anchor
Malaria
Plasmodium vivax.
protozoan
dna
protozoan
tertiary
Antigens
Dna
Protein structure
Sequence analysis
Rights
License
Abierto (Texto Completo)
Description
Summary:Plasmodium vivax malaria remains one of the tropical diseases causing an enormous burden on global public health. Several proteins located on this parasite species' merozoite surface have been considered the most suitable antigens for being included in an anti-malarial vaccine, given the functional role they play during the parasite's interaction with red blood cells. The present study identifies and characterizes the P. vivax Pv12 surface protein which was evaluated by using molecular biology and immunochemistry assays; its antigenic potential was also examined in natural and experimental P. vivax malaria infections. The P. vivax VCG-1 strain Pv12 gene encodes a 362 amino acid-long protein exhibiting a signal peptide, a glycosylphosphatidylinositol (GPI) anchor sequence and two 6-Cys domains. The presence of the Pv12 protein on the parasite's surface and its association with detergent-resistant membrane complexes, together with its antigenic potential, supports the notion that this antigen could play an important role as a red blood cell binding ligand. Further studies aimed at establishing the immunogenicity and protection-inducing ability of the Pv12 protein or its products in the Aotus experimental model are thus suggested. © 2012 Elsevier GmbH.