Monoclonal antibodies (McAbs) generated against rhamnogalacturonan I (RC-I) purified from suspension-cultured sycamore maple (Acer pseudoplafanus) cells fall into three recognition groups. Four McAbs (group I) recognize an epitope that appears to be immunodominant and is present on RC-I from maize and sycamore maple, pectin and polygalacturonic acid from citrus, gum tragacanth, and membrane glycoproteins from suspension-cultured cells of maize, tobacco, parsley, bean, and sycamore maple. A second set of McAbs (group II) recognizes an epitope present in sycamore maple RC-I but does not bind to any of the other polysaccharides or glycoproteins recognized by group 1. Lastly, one McAb, CCRC-M1 (group III), binds to RC-I and more strongly to xyloglucan (XC) from sycamore maple but not to maize RC-I, citrus polygaladuronic acid, or to the plant membrane glycoproteins recognized by group 1. lhe epitope to which CCRC-M1 binds has been examined in detail. Ligand competition assays using a series of oligosaccharides derived from or related to sycamore maple XC demonstrated that a terminal a-(142)-linked fucosyl residue constitutes an essentia1 part of the epitope recognized by CCRC-M1. Oligosaccharides containing this structural motif compete with intact sycamore maple XC for binding to the antibody, whereas structurally related oligosaccharides, which do not contain terminal fucosyl residues or in which the terminal fucosyl residue is linked a-(1+3) to the adjacent glycosyl residue, do not compete for the antibody binding site. lhe ligand binding assays also indicate that CCRC-M1 binds to a conformationally dependent structure of the polysaccharide. Other results of this study establish that some of the carbohydrate

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