Identification of conserved erythrocyte binding regions in members of the Plasmodium falciparum Cys6 lipid raft-associated protein family

Detergent-resistant lipid raft membrane-associated Pf12, Pf38 and Pf41 proteins belong to the Cys6 family, whose members are implicated in Plasmodium falciparum invasion to erythrocytes. We have analyzed the interaction between 20-mer-long synthetic peptides spanning the entire Pf12, Pf38 and Pf41 sequences and erythrocytes. Eight high-activity binding peptides (HABPs) were identified in these proteins, which presented saturable bindings susceptible to erythrocytes' enzymatic treatment, and ?-turn, random coil and ?-helical elements as principal structural features. Some of these HABPs inhibited merozoite invasion in vitro, suggesting a possible role of Pf12, Pf38 and Pf41 during erythrocyte invasion and supporting their inclusion in the design of a fully effective antimalarial vaccine. © 2009 Elsevier Ltd. All rights reserved.

• Fecha de publicación: 2009
• Institución: Universidad del Rosario
• Repositorio: Repositorio EdocUR - U. Rosario
• Idioma: eng
• OAI Identifier: oai:repository.urosario.edu.co:10336/23451
• Acceso en línea: https://doi.org/10.1016/j.vaccine.2009.04.039; https://repository.urosario.edu.co/handle/10336/23451
• Palabra clave: Alanylglycyllysylvalylasparaginylasparaginyllysylvalyl cysteinyllysylisoleucylglutaminylglycyllysylprolylglycylglutamyll eucylvalylglycine; Alanylleucylasparaginylarginylphenylalanyllysyllysyl methionyllysylaspartylleucylseryllysylphenylalanylphenylalanyl asparaginylaspartylglutaminylalanylaspartic acid; Asparaginylthreonylthreonyllysylleucylasparaginylleucyl prolyllysylserylleucylasparaginylisoleucylprolylasparaginylaspartyl isoleucylleucylasparaginyltyrosinel; Cysteine derivative; Leucylhistidyllysylasparaginyllysylvalylthreonylaspartyll eucyllysylthreonylleucylisoleucylprolylglycyltyrosylalanylseryltyrosylthreonine; Malaria vaccine; Membrane protein; Methionylaspartylhistidyltyrosylasparaginylasparaginyl threonylphenylalanyltyrosylserylarginylleucylprolylserylleucyl isoleucylserylaspartylasparaginyltryptophan; Peptide derivative; Pf12 protein; Pf38 protein; Pf41 protein; Tyrosylserylisoleucyllysylprolylaspartylglycylcysteinylphenyl alanylserylasparaginylvalyltyrosylvalyllysylarginyltyrosylprolyl asparaginylglutamine; Unclassified drug; Valylisoleucylglycylserylserylmethionylphenylalanylmethionyl arginylarginylserylleucylthreonylprolylasparaginyllysylisoleucyl asparaginylglutamylvaline; Valylleucylarginylisoleucylhistidylisoleucylserylasparaginyl glycylvalylleucylarginyllysylisoleucylprolylglycylcysteinyl aspartylphenylalanylasparagine; Alpha helix; Article; Beta turn; Binding affinity; Binding site; Erythrocyte; Host parasite interaction; Human; Human cell; Lipid raft; Malaria; Merozoite; Plasmodium falciparum; Priority journal; Protein analysis; Protein function; Animals; Erythrocytes; Humans; Plasmodium falciparum; Protein binding; Protein interaction mapping; Protozoan proteins; Antimalarial vaccine; Cys6 family; High-activity binding peptides; Pf12; Pf38; Pf41; Plasmodium falciparum; tertiary; secondary; protozoan; cell surface; Antigens; Protein structure; Protein structure; Receptors
• License: Abierto (Texto Completo)