Demonstration of a Surface Antigen of Clostridium tyrobutyricum by Use of Immunoblotting with a Monoclonal Antibody

• Published in: MICROBIOLOGY and IMMUNOLOGY Vol. 34; no. 1; pp. 55 - 64
• Main Authors: Gueguen, Françoise, Robreau, Georges, Talbot, Françoise, Malcoste, Roger
• Format: Journal Article
• Language: English
• Published: Tokyo Blackwell Publishing Ltd 01.01.1990; Center For Academic Publications Japan; Center for Academic Publications Japan
• Subjects: Antibodies, Monoclonal; Antigens, Bacterial - analysis; Antigens, Surface - analysis; Bacteriology; Biological and medical sciences; Blotting, Western - methods; Cell Wall - immunology; Clostridium - immunology; Clostridium tyrobutyricum; Enzyme-Linked Immunosorbent Assay; Fundamental and applied biological sciences. Psychology; Hot Temperature; Microbiology; Morphology, structure, chemical composition; Phenols; Antigenic determinant; Gel electrophoresis; Clostridium tyrobutyricum; Clostridiales; Monoclonal antibody; Cell surface; Antigen; Clostridiaceae; Lipopolysaccharide; Immunoblotting assay; Bacteria; Carbohydrate; Detection
• ISSN: 0385-5600; 1348-0421
• DOI: 10.1111/j.1348-0421.1990.tb00991.x

A monoclonal antibody, prepared against whole cells of Clostridium tyrobutyricum, recognized a surface antigen extracted by heat treatment or by hot phenol-water treatment. This antigen, after analysis by polyacrylamide gel electrophoresis and immunoblotting, has been shown to present a regularly-spaced ladder pattern similar to those shown by the lipopolysaccharide of many gram-negative bacteria. The proteinase K has been shown to have no effect on the recognition of this epitope by the monoclonal antibody. On the contrary, the inhibition of the antigen reactivity to the monoclonal antibody after a mild periodate oxidation suggests the involvement of a carbohydrate moiety in the epitope. Moreover, the SDS-PAGE analysis of phenol-water extracts has shown an additional compound, detected by silver staining but not recognized by the monoclonal antibody.