Skip Navigation



Glycobiology Advance Access published online on March 24, 2004
Glycobiology, doi:10.1093/glycob/cwh077
This Article
Right arrow Advance Access manuscript (PDF) Freely available
Right arrow All Versions of this Article:
14/7/635    most recent
cwh077v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Muthusamy, A.
Right arrow Articles by Gowda, C. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Muthusamy, A.
Right arrow Articles by Gowda, C. D.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Submitted on January 21, 2004
Accepted on March 10, 2004

© 2004 Glycobiology © Oxford University Press 2004; all rights reserved.

ORIGINAL ARTICLES

Structural characterization of the bovine tracheal chondroitin sulfate chains and binding of Plasmodium falciparum-infected erythrocytes

Arivalagan Muthusamy 1, Rajeshwara N. Achur 1, Manojkumar Valiyaveettil 1, Subbarao V. Madhunapantula 1, Ikuko Kakizaki 1, Veer P. Bhavanandan 1, and Channe D. Gowda 1*

1 Department of Biochemistry and Molecular Biology, Pennsylvania State University College of Medicine, Hershey, PA 17033, USA

* To whom correspondence should be addressed. E-mail: gowda{at}psu.edu.

Abstract

Sequestration of Plasmodium falciparum-infected red blood cells (IRBCs) in the human placenta is mediated by chondroitin 4-sulfate (C4S). A cytoadherence assay using chondroitin sulfate proteoglycans (CSPGs) is widely used for studying C4S-IRBC interactions. Bovine tracheal chondroitin sulfate A (CSA) preparation lacking a major portion of core protein has been frequently used for the assay. Here, the CSPG purified from bovine trachea and CSA were assessed for IRBC binding, and the CS chains studied in detail for structure/activity relationship. The IRBCs bound at significantly higher density to the CSPG than CSA. The CS chains of CSPG/CSA are heterogeneous with varying levels of 4- and 6-sulfates, which are distributed such that ~80% of the 4-sulfated disaccharides are present as single and blocks of two or three separated by one to three 6-sulfated disaccharides. The remainder of the 4-sulfated disaccharides is present in blocks comprised of 4 to 12 units, separated by 6-sulfated disaccharides. In the IRBC adherence inhibition analysis, CSA fragments with 88-92% 4-sulfate were significantly less inhibitory than the intact CSA, indicating that the regions consisting of shorter 4-sulfated blocks efficiently bind IRBCs despite the presence of relatively high levels of 6-sulfate. This is because the 6-sulfated disaccharides have unsubstituted C-4 hydroxyls that are crucial for IRBC binding. The presence of high levels of 6-sulfate, however, significantly interfere with the IRBC binding activity of CSA, which otherwise would more efficiently bind IRBCs. Thus, our study revealed the distribution pattern of 4- and 6-sulfate in bovine tracheal CSA and structural basis for IRBC binding.


bovine tracheal chondroitin sulfate proteoglycan, chondroitin sulfate chains, infected erythrocytes adherence, Plasmodium falciparum, structure-adherence relationship
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
M. Ueyama, H. Takemae, Y. Ohmae, H. Yoshida, H. Toyoda, R. Ueda, and S. Nishihara
Functional Analysis of Proteoglycan Galactosyltransferase II RNA Interference Mutant Flies
J. Biol. Chem., March 7, 2008; 283(10): 6076 - 6084.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Pathol.Home page
A. Muthusamy, R. N. Achur, M. Valiyaveettil, J. J. Botti, D. W. Taylor, R. F. Leke, and D. C. Gowda
Chondroitin Sulfate Proteoglycan but Not Hyaluronic Acid Is the Receptor for the Adherence of Plasmodium falciparum-Infected Erythrocytes in Human Placenta, and Infected Red Blood Cell Adherence Up-Regulates the Receptor Expression
Am. J. Pathol., June 1, 2007; 170(6): 1989 - 2000.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. S. P. Gowda, S. V. Madhunapantula, R. N. Achur, M. Valiyaveettil, V. P. Bhavanandan, and D. C. Gowda
Structural Basis for the Adherence of Plasmodium falciparum-infected Erythrocytes to Chondroitin 4-Sulfate and Design of Novel Photoactivable Reagents for the Identification of Parasite Adhesive Proteins
J. Biol. Chem., January 12, 2007; 282(2): 916 - 928.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.