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Characterization of anti-heparan sulfate phage display antibodies AO4B08 and HS4E4
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
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2007 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 282, no 29, 21032-21042 p.Article in journal (Refereed) Published
Abstract [en]

Heparan sulfates (HS) are linear carbohydrate chains, covalently attached to proteins, that occur on essentially all cell surfaces and in extracellular matrices. HS chains show extensive structural heterogeneity and are functionally important during embryogenesis and in homeostasis due to their interactions with various proteins. Phage display antibodies have been developed to probe HS structures, assess the availability of protein-binding sites, and monitor structural changes during development and disease. Here we have characterized two such antibodies, AO4B08 and HS4E4, previously noted for partly differential tissue staining. AO4B08 recognized both HS and heparin, and was found to interact with an ubiquitouys, N-, 2-O-, and 6-O-sulfated saccharide motif, including an internal 2-O-sulfate group. HS4E4 turned out to preferentially recognize low-sulfated HS motifs containing iduronic acid, and N-sulfated as well as N-acetylated glucosamine residues. Contrary to AO4B08, HS4E4 did not bind highly O-sulfated structures such as found in heparin.

Place, publisher, year, edition, pages
2007. Vol. 282, no 29, 21032-21042 p.
Keyword [en]
Amino Acid Motifs, Animals, Antibodies/*chemistry, Binding Sites, CHO Cells, Cricetinae, Cricetulus, Epitopes/chemistry, Glucosamine/chemistry, Heparitin Sulfate/*chemistry/immunology, Iduronic Acid/chemistry, Peptide Library, Polysaccharides/chemistry, Protein Binding, Protein Structure; Tertiary
National Category
Medical and Health Sciences Biological Sciences Chemical Sciences
URN: urn:nbn:se:uu:diva-15764DOI: 10.1074/jbc.M702073200ISI: 000248047500030PubMedID: 17517889OAI: oai:DiVA.org:uu-15764DiVA: diva2:43535
Available from: 2008-03-05 Created: 2008-03-05 Last updated: 2011-02-05Bibliographically approved

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Publisher's full textPubMedhttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Retrieve&list_uids=17517889&dopt=Citation

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Li, Jin-PingLindahl, UlfSpillmann, Dorothe
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