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Malaria parasite survival depends on conserved binding peptides’ critical biological functions
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Autores
Patarroyo M.E.
Arévalo-Pinzón G.
Reyes C.
Moreno-Vranich A.
Patarroyo M.A.
Fecha
2016
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Caister Academic Press
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Abstract
Biochemical, structural and single amino acid level analysis of 49 Plasmodium falciparum protein regions (13 sporozoite and 36 merozoite proteins) has highlighted the functional role of each conserved high activity binding peptide (cHABP) in cell host-microbe interaction, involving biological functions such as gliding motility, traversal activity, binding invasion, reproduction, nutrient ion transport and the development of severe malaria. Each protein's key function in the malaria parasite's asexual lifecycle (pre-erythrocyte and erythro-cyte) is described in terms of cHABPs; their sequences were located in elegant work published by other groups regarding critical binding regions implicated in malarial parasite invasion. Such cHABPs represent the starting point for developing a logical and rational methodology for selecting an appropriate mixture of modified cHABPs to be used in a completely effective, synthetic antimalarial vaccine. Such methodology could be used for developing vaccines against diseases scourging humanity. © 2016, Caister Academic Press. All rights reserved.
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Keywords
Calcium ion , falciparum , Epidermal growth factor , Erythrocyte membrane protein 1 , Membrane protein , Microorganism protein , Protein clag 3 2 , Protein csp 1 , Protein msp1 , Protein msp2 , Protein pf12 , Protein pf38 , Protein pf41 , Protein pfrh , Protein ptramp , Protein rama , Protein rh2a , Protein rh2b , Protein rh4 , Protein rhoph3 , Sialic acid , Unclassified drug , Peptide , Protozoal protein , Amino acid sequence , Article , Binding site , Disease association , Erythrocyte , Host parasite interaction , Human , Liver , Malaria , Merozoite , Nonhuman , Parasite migration , Parasite survival , Plasmodium falciparum , Protein binding , Protein domain , Protein expression , Regulatory mechanism , Sporozoite , Tight junction , Hep-g2 cell line , Host parasite interaction , Malaria falciparum , Parasitology , Physiology , Plasmodium falciparum , Erythrocytes , Hep g2 cells , Host-parasite interactions , Humans , Malaria , Peptides , Plasmodium falciparum , Protozoan proteins , Sporozoites
