Characterization of a monoclonal antibody that recognizes an arabinosylated (1 → 6)-β-d-galactan epitope in plant complex carbohydrates
✍ Scribed by Wolfram Steffan; Pavol Kovácč; Peter Albersheim; Alan G. Darvill; Michael G. Hahn
- Publisher
- Elsevier Science
- Year
- 1995
- Tongue
- English
- Weight
- 709 KB
- Volume
- 275
- Category
- Article
- ISSN
- 0008-6215
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✦ Synopsis
Monoclonal antibody CCRC-M7 is representative of a group of antibodies with similar binding specificity that were generated using the plant cell-wall pectic polysaccharide, rhamnogalacturonan I, as immunogen. The epitope recognized by CCRC-M7 is present in several plant polysaccharides and membrane glycoproteins. Selective enzymatic or chemical removal of arabinosyl residues from rhamnogalacturonan I reduced, but did not abolish, the ability of CCRC-M7 to bind to the polysaccharide. In contrast, enzymatic removal of both arabinosyl and galactosyl residues from rhamnogalacturonan I completely abolished binding of CCRC-M7 to the resulting polysaccharide. Competitive ELISAs using chemically defined oligosaccharides to compete for the CCRC-M7 binding site showed that oligosaccharides containing (1-->6)-linked beta-D-galactosyl residues were the best competitors among those tested, with the tri-, penta-, and hexa-saccharides being equally effective. The combined results from indirect and competitive ELISAs suggest that the minimal epitope recognized by CCRC-M7 encompasses a (1-->6)-linked beta-galactan containing at least three galactosyl residues with at least one arabinosyl residue attached.