scholarly journals Characterization of Proteoglycans of Human Placenta and Identification of Unique Chondroitin Sulfate Proteoglycans of the Intervillous Spaces That Mediate the Adherence ofPlasmodium falciparum-infected Erythrocytes to the Placenta

2000 ◽  
Vol 275 (51) ◽  
pp. 40344-40356 ◽  
Author(s):  
Rajeshwara N. Achur ◽  
Manojkumar Valiyaveettil ◽  
Abdulnaser Alkhalil ◽  
Christian F. Ockenhouse ◽  
D. Channe Gowda
Keyword(s):  
Chondroitin Sulfate ◽  
Human Placenta ◽  
Chondroitin Sulfate Proteoglycans ◽  
Ofplasmodium Falciparum

scholarly journals Structural Requirements for the Adherence ofPlasmodium falciparum-infected Erythrocytes to Chondroitin Sulfate Proteoglycans of Human Placenta

2000 ◽  
Vol 275 (51) ◽  
pp. 40357-40364 ◽  
Author(s):  
Abdulnaser Alkhalil ◽  
Rajeshwara N. Achur ◽  
Manojkumar Valiyaveettil ◽  
Christian F. Ockenhouse ◽  
D. Channe Gowda
Keyword(s):  
Chondroitin Sulfate ◽  
Human Placenta ◽  
Chondroitin Sulfate Proteoglycans ◽  
Structural Requirements ◽  
Ofplasmodium Falciparum

scholarly journals An affinity chromatography and glycoproteomics workflow to profile the chondroitin sulfate proteoglycans that interact with malarial VAR2CSA in the placenta and in cancer

Glycobiology ◽  
2020 ◽  
Vol 30 (12) ◽  
pp. 989-1002 ◽  
Author(s):  
Alejandro Gómez Toledo ◽  
Jessica Pihl ◽  
Charlotte B Spliid ◽  
Andrea Persson ◽  
Jonas Nilsson ◽  
...  
Keyword(s):  
Chondroitin Sulfate ◽  
Affinity Purification ◽  
Chondroitin Sulfate Proteoglycans ◽  
Intervillous Space ◽  
Core Proteins ◽  
Heterogenous Group ◽  
Tumor Tissues ◽  
Infected Cells ◽  
Cancer Tissues

Abstract Chondroitin sulfate (CS) is the placental receptor for the VAR2CSA malaria protein, expressed at the surface of infected erythrocytes during Plasmodium falciparum infection. Infected cells adhere to syncytiotrophoblasts or get trapped within the intervillous space by binding to a determinant in a 4-O-sulfated CS chains. However, the exact structure of these glycan sequences remains unclear. VAR2CSA-reactive CS is also expressed by tumor cells, making it an attractive target for cancer diagnosis and therapeutics. The identities of the proteoglycans carrying these modifications in placental and cancer tissues remain poorly characterized. This information is clinically relevant since presentation of the glycan chains may be mediated by novel core proteins or by a limited subset of established proteoglycans. To address this question, VAR2CSA-binding proteoglycans were affinity-purified from the human placenta, tumor tissues and cancer cells and analyzed through a specialized glycoproteomics workflow. We show that VAR2CSA-reactive CS chains associate with a heterogenous group of proteoglycans, including novel core proteins. Additionally, this work demonstrates how affinity purification in combination with glycoproteomics analysis can facilitate the characterization of CSPGs with distinct CS epitopes. A similar workflow can be applied to investigate the interaction of CSPGs with other CS binding lectins as well.

Isolation and characterization of chondroitin sulfate proteoglycans from porcine thoracic aorta

1986 ◽  
Vol 883 (1) ◽  
pp. 83-90 ◽  
Author(s):  
Junichiro Aikawa ◽  
Mamoru Isemura ◽  
Hiroshi Munakata ◽  
Noboru Ototani ◽  
Chie Kodama ◽  
...  
Keyword(s):  
Chondroitin Sulfate ◽  
Thoracic Aorta ◽  
Chondroitin Sulfate Proteoglycans ◽  
Isolation And Characterization

Structural insights into chondroitin sulfate binding in pregnancy-associated malaria

2010 ◽  
Vol 38 (5) ◽  
pp. 1337-1341 ◽  
Author(s):  
Pongsak Khunrae ◽  
Matthew K. Higgins
Keyword(s):  
Chondroitin Sulfate ◽  
Infected Erythrocyte ◽  
Binding Pocket ◽  
Chondroitin Sulfate Proteoglycans ◽  
Ligand Specificity ◽  
Erythrocyte Surface ◽  
Malaria During Pregnancy ◽  
Structural Insights ◽  
Major Target

Malaria during pregnancy is caused when parasite-infected erythrocytes accumulate within the placenta through interactions between the VAR2CSA protein on the infected erythrocyte surface and placental CSPGs (chondroitin sulfate proteoglycans). This interaction is the major target for therapeutics to treat or prevent pregnancy-associated malaria. Here we review the structural characterization of CSPG-binding DBL (Duffy-binding like) domains from VAR2CSA and summarize the growing evidence that the exquisite ligand specificity of VAR2CSA results from the adoption of higher-order architecture in which these domains fold together to form a ligand-binding pocket.

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