Characterization of the wheat germ agglutinin-binding property of Treponema denticola.
Lectins were used to characterize glycoconjugates on the cell surface of Treponema denticola, a suspected periodontopathogen. Bacteria were first screened by light microscopy using fluorescein isothiocyanate-coupled lectins. Wheat germ agglutinin (WGA) showed a high reactivity to T. denticola. While the WGA-binding activity was accentuated following heating or detergent treatments of bacterial cells, the reaction was inhibited by incorporation of competing carbohydrates. Scanning and transmission electron microscope studies were conducted in order to characterize the distribution of the WGA-binding sites on the cell surface of T. denticola. Data from these studies confirmed that heat treatment increases the percentage of labeled profiles and suggest that the WGA-binding sites are concentrated on specific regions on the spirochete surface. Initial biochemical analysis indicated that the high reactivity to WGA resides in a peptidoglycan fraction.
Département de Santé Buccale, Faculté de Médecine Dentaire, Université de Montréal, Québec, Canada.
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D001422:Bacterial Adhesion; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000302:isolation & purification; D016650:Fluorescein-5-isothiocyanate; D006046:Gold; D015151:Immunoblotting; D008562:Membrane Glycoproteins / Q000737:chemistry* / Q000302:isolation & purification; D008854:Microscopy, Electron; D010059:Ovomucin; D010457:Peptidoglycan / Q000302:isolation & purification; D011975:Receptors, Mitogen / Q000737:chemistry*; D014208:Treponema / Q000737:chemistry* / Q000648:ultrastructure*; D014909:Wheat Germ Agglutinins / Q000378:metabolism*
D001425:Bacterial Outer Membrane Proteins; D008562:Membrane Glycoproteins; D010457:Peptidoglycan; D011975:Receptors, Mitogen; D014909:Wheat Germ Agglutinins; C027503:wheat germ agglutinin receptor; D010059:Ovomucin; D006046:Gold; D016650:Fluorescein-5-isothiocyanate