Identifying Plasmodium Falciparum Merozoite Surface Antigen 3 (MSP3) Protein Peptides That Bind Specifically to Erythrocytes and Inhibit Merozoite Invasion

Overview

Journal Protein Sci

Specialty Biochemistry

Date 2005 Jul 1

PMID 15987906

Citations 13

Authors

Luis E Rodriguez

Hernando Curtidor

Marisol Ocampo

Javier Garcia

Alvaro Puentes

John Valbuena

Ricardo Vera

Ramses Lopez

Manuel E Patarroyo

Affiliations

Soon will be listed here.

Abstract

Receptor-ligand interactions between synthetic peptides and normal human erythrocytes were studied to determine Plasmodium falciparum merozoite surface protein-3 (MSP-3) FC27 strain regions that specifically bind to membrane surface receptors on human erythrocytes. Three MSP-3 protein high activity binding peptides (HABPs) were identified; their binding to erythrocytes became saturable, had nanomolar affinity constants, and became sensitive on being treated with neuraminidase and trypsin but were resistant to chymotrypsin treatment. All of them specifically recognized 45-, 55-, and 72-kDa erythrocyte membrane proteins. They all presented alpha-helix structural elements. All HABPs inhibited in vitro P. falciparum merozoite invasion of erythrocytes by ~55%-85%, suggesting that MSP-3 protein's role in the invasion process probably functions by using mechanisms similar to those described for other MSP family antigens.

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