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Monoclonal antibodies to the carbohydrate structure Lewisx stimulate the adhesive activity of leukocyte integrin CD11b/CD18 (CR3, Mac‐1, αmβ2) on human granulocytes

Several carbohydrate structures on human granulocytes have been discussed as potential ligands for C‐ type lectins (selectins) on endothelial cells. Among them are the lacto‐series type II chain antigens sialyl‐Lewisx (SLex), Lewisx (Lex), and VIM2. We demonstrated in this study that monoclonal antibodies (mAbs) to Lex and to SLex, but not other anticarbohydrate mAbs (VIM2, CDwl7, CD24), can stimulate granulocytes to form homotypic aggregates. This effect was particularly noticeable with three distinct anti‐Lex mAbs (3C6, 4D1, 6C7). Much less impressive effects were also seen with nine other anti‐Lex mAbs and with the anti‐SLex mAb CSLEX1. Aggregation was shown to be an active process. It is temperature and energy dependent, requires divalent cations, and is selective in terms of mAb specificity. Anti‐ Lex‐induced homoaggregate formation could be inhibited with CDllb mAb JML‐H11 and CD54 (ICAM1) mAb LB‐2 and thus seems to be associated with activation of the β2‐integrin cytoadhesion pathway.