Demonstration of peptidoglycan-binding sites on lymphocytes and macrophages by photoaffinity cross-linking.

摘要: One dominant binding site (70 kDa 6.5 pI protein) for bacterial cell wall peptidoglycan (PGN), a macrophage activator and polyclonal B mitogen, was demonstrated on mouse T lymphocytes macrophages by photoaffinity cross-linking two-dimensional polyacrylamide gel electrophoresis. This not present erythrocytes. The specific polymeric PGN competitively inhibited unlabeled with IC50 = 48 micrograms/ml (0.38 microM). partially O-acetylated monomers (IC50 469 micrograms/ml, 521 microM), dextran sulfate 1024 124 (GlcNAc)3 6.6 mg/ml, 10 mM), non-O-acetylated dimers, muramyl dipeptide, pentapeptide, GlcNAc, teichoic acid, protein A, gelatin. surface location of the 70-kDa PGN-binding indicated ability to bind this in intact metabolically inactive cells (at 4 degrees C presence 0.1% NaN3) extract from viable noncytotoxic concentration n-octyl-beta-D-glucopyranoside.