How specific is Plasmodium falciparum adherence to chondroitin 4-sulfate?

被引：6
|
作者：
Goel, Suchi [1 ]
Gowda, D. Channe [1 ]
机构：
[1] Penn State Univ, Coll Med, Dept Biochem & Mol Biol, Hershey, PA 17033 USA
来源：
TRENDS IN PARASITOLOGY | 2011年 / 27卷 / 09期
基金：
美国国家卫生研究院;
关键词：
ERYTHROCYTE-MEMBRANE PROTEIN-1; PREGNANCY-ASSOCIATED MALARIA; VARIANT SURFACE-ANTIGENS; INFECTED ERYTHROCYTES; SULFATE PROTEOGLYCANS; HUMAN PLACENTA; STRUCTURAL BASIS; PARASITE ADHESION; PROTECTIVE IMMUNITY; BINDING DOMAIN;
D O I：
10.1016/j.pt.2011.03.005
中图分类号：
R38 [医学寄生虫学]; Q [生物科学];
学科分类号：
07 ; 0710 ; 09 ; 100103 ;
摘要：
Plasmodium falciparum infection during pregnancy results in the sequestration of infected red blood cells (IRBCs) in the placenta, contributing to pregnancy associated malaria (PAM). IRBC adherence is mediated by the binding of a variant Plasmodium falciparum erythrocyte binding protein 1 named VAR2CSA to the low sulfated chondroitin 4-sulfate (C4S) proteoglycan (CSPG) present predominantly in the intervillous space of the placenta. IRBC binding is highly specific to the level and distribution of 4-sulfate groups in C4S. Given the strict specificity of IRBC-C4S interactions, it is better to use either placental CSPG or CSPGs bearing structurally similar C4S chains in defining VAR2CSA structural architecture that interact with C4S, evaluating VAR2CSA constructs for vaccine development or studying structure-based inhibitors as therapeutics for PAM.
引用
收藏
页码：375 / 381
页数：7
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