Antigenic relationships among penicillin-binding proteins 1 from members of the families Pasteurellaceae and Enterobacteriaceae

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Abstract
Penicillin-binding proteins (PBPs) from Haemophilus influenzae RD purified by a combination of affinity chromatography, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and electroelution were used to immunize rabbits to obtain specific antisera. Antisera directed against PBP 1 (1b) of H. influenzae cross-reacted with representative organisms of the family Pasteurellaceae and with many members of the family Enterobacteriaceae but not with other gram-negative organisms. Immunization with purified PBP 3 of H. influenzae produced antisera that reacted with PBP 1 (1b) of H. influenzae and showed the same cross-reactive pattern with other species as the anti-PBP 1 antiserum. A 24,000-molecular-weight polypeptide of H. influenzae, not radiolabeled by [35S]penicillin, reacted with antisera against purified PBPs 1 (1a, 1b), 2, and 3. The results suggest that antigenic epitopes are shared among similar PBPs from related species and even among different PBPs within the same species.