Three hybridomas (P1P3, D7 and 60.5) producing monoclonal antibodies (mAbs) against lipopolysaccharide (LPS) were established. All reacted with the LPS from a typical, vaccine strain of (1414), but not with that of a variant strain (A100). Two of these mAbs (P1P3 and 60.5) cross-reacted with a LPS; only one (P1P3) reacted with a LPS. ELISA reactivities with intact LPSs, and defined partial structures covalently linked to bovine serum albumin, were compared. mAb 60.5 bound to the terminal region of a distal trisaccharide consisting of -acetylated amino sugars. D7 reacted with a substructure which can be modified in the and LPSs by addition of a polymeric O-chain. P1P3 bound to a nonacetylated glucosamine substituted with L-glycero-D-manno-heptose, present in the ‘core’ of the LPS. These mAbs may be useful for rapid typing of in clinical isolates.


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