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Adjuvant Activities in Production of Reaginic Antibody by Bacterial Cell Wall Peptidoglycan or Synthetic N-Acetylmuramyl Dipeptides in Mice

¹ Department of Microbiology and Immunology, Nippon Medical School, 1-1-5, Sendagi, Bunkyo-ku, Tokyo 113, Japan
² Department of Microbiology, Osaka University Dental School, Nakanoshima, Kita-ku, Osaka 530, Japan
³ Faculty of Science, Osaka University, Toyonaka, Osaka 560, Japan
⁴ Research and Development Division, Dainippon Pharmaceutical Co., Suita, Osaka 564, Japan

ABSTRACT

This paper is concerned with the adjuvant activity in stimulatory immunoglobulin E production against ovalbumin (OA) by bacterial cell walls, cell wall peptidoglycan (PG), and their PG fragments and synthetic N-acetylmuramyl (MurNAc) dipeptides in A/J mice. A PG isolated from Streptococcus pyogenes, PG subunit polymer and dimer obtained from Staphylococcus epidermidis, and water-soluble fragments of cell walls or PG prepared from Nocardia corynebacteriodes and Streptomyces gardneri were found to enhance both the primary and secondary responses of anti-OA immunoglobulin E antibody production. It was suggested that the PG portion, either intact or highly degraded, was capable of enhancing the immunoglobulin E antibody production, and there was no need for the non-PG moiety or intactness of PG structure for the adjuvant activity. This finding was confirmed and extended by the use of synthetic MurNAc dipeptides. Among eight MurNAc dipeptides tested, MurNAc-L-Ala-D-isoGln, MurNAc-L-Ala-D-Gln, MurNAc-L-Ala-D-Glu, and MurNAc-L-Ser-D-isoGln were found active as an adjuvant in the stimulation of the primary and secondary reaginic anti-OA antibody production in a similar way to the cell wall PG and their fragments. None of the synthetic MurNAc-L-Ala-L-isoGln, MurNAc-L-Ala-L-Gln, MurNAc-L-Ala-L-Glu, and MurNAc-L-Ala-D-isoAsn, on the other hand, stimulated the anti-OA immunoglobulin E antibody production in either primary or secondary response, indicating the importance for the adjuvancy in immunoglobulin E production of the configuration of the glutamic acid residues adjacent to the L-Ala (or L-Ser) in muramyl dipeptides.