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The S layer of Clostridium difficile GAI 0714, which was composed of squarely arrayed, two-subunit proteins with respective molecular weights of 32 kDa and 45 kDa, was examined for its morphological, physicochemical, and biological properties. Optical diffraction analysis of the S layer showed that the surface-arrayed rhombus had four sides of 8.1 nm with interior angles of 8 8 ° . The two proteins were heterogeneous to each other in respect to the first ten N-terminal amino acid sequences except for residues No's. 4 and 9. Self-assembly of the subunit proteins into a regular array was dependent on such divalent cations as Ca2t or Zn2+, but not Ba2+ or Mg2t . When the mixture, made of purified 32 and 45 kDa subunits in an equal concentration ratio on a protein basis was submitted to self assembly, flattened paracrystalline sheetlike fragments were generated. However, neither sheetlike fragments nor regular arrays was observed for any self-assembled products derived from each subunit alone or their quantitatively heterologous mixtures. Intact cells of the organism adhered significantly to HeLa cells or mouse fibroblast 929 cells, whereas 8 M ureaor 4 M guanidinehydrochloride-extracted bacteria, from which both S layer protein subunits were removed, scarcely adhered to both cells. Fab fragments of anti-32 kDa or anti-45 kDa subunits antibodies effectively inhibited adhesion of the organism to HeLa cells, suggesting that the S layer had a direct role in adhesion.

Self-assembly, adhesion, and chemical properties of tetragonarly arrayed s-layer proteins of clostridium.