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Identifying Plasmodium falciparum merozoite surface protein-10 human erythrocyte specific binding regions

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Puentes, Alvaro
Ocampo, Marisol
Rodríguez, Luis Eduardo
Vera, Ricardo
Valbuena, John
Curtidor, Hernando
García, Javier
López, Ramsés
Tovar, Diana
Cortes, Jimena

Fecha
2005-05

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Elsevier

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Abstract
Receptor-ligand interactions between synthetic peptides and normal human erythrocytes were studied to determine P. falciparum merozoite surface protein-10 (MSP-10) regions specifically binding to membrane surface receptors on human erythrocytes. Three MSP-10 protein High Activity Binding Peptides (HABPs) were identified, whose binding to erythrocytes became saturable and sensitive on being treated with neuraminidase, trypsin and chymotrypsin. Some of them specifically recognised a 50 kDa erythrocyte membrane protein. Some HABPs inhibited in vitro P. falciparum merozoite invasion of erythrocytes by 70%, suggesting that MSP-10 protein’s possible role in the invasion process probably functions by using similar mechanisms to those described for other MSP family antigens. In addition to above results, the high homology in amino-acid sequence and superimposition of both MSP-10, MSP-8 and MSP-1 EGF-like domains and HABPs 31132, 26373 and 5501 suggest that tridimensional structure could be playing an important role in the invasion process and in designing synthetic multi-stage anti-malarial vaccines.
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Keywords
P. falciparum , Merozoite surface protein 10 , MSP-10 , High activity binding , Peptides , Invasion inhibition
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