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

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48 Scopus citations

Abstract

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

Original languageEnglish (US)
Pages (from-to)4713-4718
Number of pages6
JournalJournal of Biological Chemistry
Volume266
Issue number8
StatePublished - Jul 11 1991

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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