02407nas a2200301   4500000000100000008004100001260001300042653002600055653002700081653002400108653002800132653003800160653002000198653001300218653001600231653001300247653002500260100001500285700001500300700001500315700001600330245010000346856004100446300001100487490000700498520158600505022001402091       1997                            d  c1997 Dec10aAntibodies, Bacterial10aAntibodies, Monoclonal10aAntigens, Bacterial10aBinding Sites, Antibody10aEnzyme-Linked Immunosorbent Assay10aEpitope Mapping10aEpitopes10aGlycolipids10aKinetics10aMycobacterium leprae1 aFujiwara T1 aMinagawa F1 aSakamoto Y1 aDouglas J T00aEpitope mapping of twelve monoclonal antibodies against the phenolic glycolipid-I of M. leprae.  uhttp://ila.ilsl.br/pdfs/v65n4a07.pdf  a477-860 v653 a<p>Epitope mapping of 12 monoclonal antibodies (MAbs) directed to the trisaccharide part of the phenolic glycolipid-I (PGL-I) of Mycobacterium leprae was carried out by using the set of chemically synthesized sugar-BSA conjugates. The results can be summarized as follows: mAb (1-21), mAb (1-24) and mAb (1-25) recognized the outer (nonreducing end) monosaccharide of the trisaccharide chain of PGL-I. However, the affinity of these MAbs to the outer monosaccharide was weak. They required the contributions of some parts of the second sugar for enough affinity. MAbs ml 6A12, ml 8A2, ml 8B2, and PG2 B8F recognized the outer disaccharide. MAb F47-21-3 recognized the outer disaccharide and some parts of the third sugar. MAb SF 1 recognized the trisaccharide of PGL-I. MAb 3D1-A9 recognized the phenol group and the structure around the branching point on the carrier protein in addition to the trisaccharide. MAbs DZ 1 and 2G3-A8 had unique characters which recognized the inner part of the sugar chain. MAb DZ 1 recognized the inner (reducing end) disaccharide. MAb 2G3-A8 recognized the inner monosaccharide, phenol group and the structure around the branching point on the carrier protein. All of the MAbs tested, except for ml 6A12, recognized the anomeric configurations in the sugar parts they recognized; ml 6A12 recognized the anomeric configuration only within the outer disaccharide. This set of MAbs, which were well defined on their binding specificity, promises to be an effective tool for the immunological study of PGL-I and the clinical assessment of leprosy.</p>  a0148-916X