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

被引：28
|
作者：
Garcia, Jeison [1 ,2 ]
Curtidor, Hernando [1 ,2 ]
Pinzon, Carlos G. [1 ,2 ]
Vanegas, Magnolia [1 ,2 ]
Moreno, Armando [1 ,2 ]
Patarroyo, Manuel E. [1 ,3 ]
机构：
[1] Fdn Inst Inmunol Colombia FIDIC, Bogota, Colombia
[2] Univ Nacl Rosario, Bogota, Colombia
[3] Univ Nacl Colombia, Bogota, Colombia
来源：
VACCINE | 2009年 / 27卷 / 30期
关键词：
Antimalarial vaccine; Cys(6) family; High-activity binding peptides; Pf12; Pf38; Pf41; Plasmodium falciparum; CIRCULAR-DICHROISM SPECTRA; RED-BLOOD-CELLS; DETERGENT-RESISTANT MEMBRANES; MEROZOITE SURFACE PROTEIN-1; SECONDARY STRUCTURE; RECEPTOR INTERACTIONS; FUNCTIONAL-ANALYSIS; EBA-175; PEPTIDE; MALARIA; INVASION;
D O I：
10.1016/j.vaccine.2009.04.039
中图分类号：
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号：
100102 ;
摘要：
Detergent-resistant lipid raft membrane-associated Pf12, Pf38 and Pf41 proteins belong to the Cys(6) 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 beta-turn, random coil and alpha-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. (C) 2009 Elsevier Ltd. All rights reserved.
引用
收藏
页码：3953 / 3962
页数：10
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