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恶性疟原虫感染的红细胞与硫酸软骨素A的黏附是由恶性疟原虫红细胞膜蛋白1介导的。

The adhesion of Plasmodium falciparum-infected erythrocytes to chondroitin sulfate A is mediated by P. falciparum erythrocyte membrane protein 1.

作者信息

Reeder J C, Cowman A F, Davern K M, Beeson J G, Thompson J K, Rogerson S J, Brown G V

机构信息

The Walter and Eliza Hall Institute of Medical Research, Post Office Royal Melbourne Hospital, Victoria 3050, Australia.

出版信息

Proc Natl Acad Sci U S A. 1999 Apr 27;96(9):5198-202. doi: 10.1073/pnas.96.9.5198.

DOI:10.1073/pnas.96.9.5198
PMID:10220443
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC21841/
Abstract

Chondroitin sulfate A (CSA) is an important receptor for the sequestration of Plasmodium falciparum in the placenta, but the parasite ligand involved in adhesion has not previously been identified. Here we report the identification of a var gene transcribed in association with binding to CSA and present evidence that the P. falciparum erythrocyte membrane protein 1 product of the gene is the parasite ligand mediating CSA binding. Description of this gene and the implication of P. falciparum erythrocyte membrane protein 1 as the parasite ligand paves the way to a more detailed understanding of the pathogenesis of placental infection and potential therapeutic strategies targeting the interaction.

摘要

硫酸软骨素A(CSA)是疟原虫在胎盘内滞留的重要受体,但此前尚未鉴定出参与黏附的寄生虫配体。在此,我们报告了一个与结合CSA相关转录的var基因的鉴定,并提供证据表明该基因的恶性疟原虫红细胞膜蛋白1产物是介导CSA结合的寄生虫配体。对该基因的描述以及恶性疟原虫红细胞膜蛋白1作为寄生虫配体的意义,为更详细地了解胎盘感染的发病机制以及针对该相互作用的潜在治疗策略铺平了道路。

相似文献

1
The adhesion of Plasmodium falciparum-infected erythrocytes to chondroitin sulfate A is mediated by P. falciparum erythrocyte membrane protein 1.恶性疟原虫感染的红细胞与硫酸软骨素A的黏附是由恶性疟原虫红细胞膜蛋白1介导的。
Proc Natl Acad Sci U S A. 1999 Apr 27;96(9):5198-202. doi: 10.1073/pnas.96.9.5198.
2
Sequestration of Plasmodium falciparum-infected erythrocytes to chondroitin sulfate A, a receptor for maternal malaria: monoclonal antibodies against the native parasite ligand reveal pan-reactive epitopes in placental isolates.恶性疟原虫感染的红细胞与硫酸软骨素A(一种母婴疟疾的受体)的结合:针对天然寄生虫配体的单克隆抗体揭示了胎盘分离物中的泛反应性表位。
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3
Cross-reactive surface epitopes on chondroitin sulfate A-adherent Plasmodium falciparum-infected erythrocytes are associated with transcription of var2csa.硫酸软骨素A粘附的恶性疟原虫感染红细胞上的交叉反应性表面表位与var2csa的转录相关。
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Placenta cryosections for study of the adhesion of Plasmodium falciparum-infected erythrocytes to chondroitin sulfate A in flow conditions.用于研究恶性疟原虫感染的红细胞在流动条件下与硫酸软骨素A黏附的胎盘冷冻切片。
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Identification of glycosaminoglycan binding domains in Plasmodium falciparum erythrocyte membrane protein 1 of a chondroitin sulfate A-adherent parasite.硫酸软骨素A黏附型疟原虫恶性疟原虫红细胞膜蛋白1中糖胺聚糖结合结构域的鉴定
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Selective upregulation of a single distinctly structured var gene in chondroitin sulphate A-adhering Plasmodium falciparum involved in pregnancy-associated malaria.在与妊娠相关疟疾中涉及的硫酸软骨素A黏附恶性疟原虫中,单个结构独特的var基因的选择性上调。
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VAR2CSA is the principal ligand for chondroitin sulfate A in two allogeneic isolates of Plasmodium falciparum.VAR2CSA是恶性疟原虫两个同种异体分离株中硫酸软骨素A的主要配体。
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Antibodies from malaria-exposed pregnant women recognize trypsin resistant epitopes on the surface of Plasmodium falciparum-infected erythrocytes selected for adhesion to chondroitin sulphate A.来自接触过疟疾的孕妇的抗体能够识别恶性疟原虫感染的红细胞表面上对胰蛋白酶具有抗性的表位,这些红细胞是被选择用于黏附硫酸软骨素A的。
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Maternal antibodies block malaria.母体抗体可抵御疟疾。
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Blood. 1998 Jun 15;91(12):4803-9.
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PECAM-1/CD31, an endothelial receptor for binding Plasmodium falciparum-infected erythrocytes.PECAM-1/CD31,一种用于结合恶性疟原虫感染红细胞的内皮受体。
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Identification of a region of PfEMP1 that mediates adherence of Plasmodium falciparum infected erythrocytes to CD36: conserved function with variant sequence.鉴定恶性疟原虫感染红细胞与CD36结合的PfEMP1区域:功能保守但序列可变
Blood. 1997 Nov 1;90(9):3766-75.
9
Chondroitin sulfate of thrombomodulin is an adhesion receptor for Plasmodium falciparum-infected erythrocytes.血栓调节蛋白的硫酸软骨素是恶性疟原虫感染红细胞的黏附受体。
Mol Biochem Parasitol. 1997 Sep;88(1-2):267-71. doi: 10.1016/s0166-6851(97)00082-0.
10
Plasmodium falciparum-infected erythrocytes adhere to the proteoglycan thrombomodulin in static and flow-based systems.恶性疟原虫感染的红细胞在静态和基于流动的系统中会黏附于蛋白聚糖血栓调节蛋白。
Exp Parasitol. 1997 May;86(1):8-18. doi: 10.1006/expr.1996.4142.