Purification and characterization of a novel type of fimbriae from the oral anaerobe Bacteroides gingivalis

Fimbriae and their constituent protein (fimbrilin) were purified to homogeneity from the bacterial wash fluid and cell lysate fraction, respectively, of Bacteroides gingivalis 381. Fimbriae, observed by negative staining, were curly, single-stranded filaments with a diameter of ca. 5 nm. The apparent molecular weight of the fimbrilin was 43,000. Fimbriae were resistant to sodium dodecyl sulfate denaturation at 70 degrees C. Heating at 100 degrees C in sodium dodecyl sulfate was needed to completely dissociate them to monomers of fimbrilin. Different sets of antigenic determinants seemed to be exposed on the surfaces of fimbriae and sodium dodecyl sulfate-denatured fimbrilin. Purified fimbriae did not show either hemagglutinating activity or hemagglutination inhibitory activity, although it has been inferred on the basis of circumstantial evidence that fimbriae are correlated to hemagglutinating activity of the organism. Hemagglutinin activity, however, was detected in culture supernatant, and this observation suggests that fimbriae of a different type or a lectin-like protein may be acting as hemagglutinin in B. gingivalis.

[1]  J. Salk.  A Simplified Procedure for Titrating Hemagglutinating Capacity of Influenza-Virus and the Corresponding Antibody , 1944, The Journal of Immunology.

[2]  O. H. Lowry,et al.  Protein measurement with the Folin phenol reagent. , 1951, The Journal of biological chemistry.

[3]  J. Lowy,et al.  The structure of F-actin and of actin filaments isolated from muscle , 1963 .

[4]  K. Okuda,et al.  Haemagglutinating activity of Bacteroides melaninogenicus. , 1974, Archives of oral biology.

[5]  J. Ottow.  Ecology, physiology, and genetics of fimbriae and pili. , 1975, Annual review of microbiology.

[6]  B. Lugtenberg,et al.  Electrophoretic resolution of the ‘major outer membrane protein’ of Escherichia coli K12 into four bands , 1975, FEBS letters.

[7]  M. Simon,et al.  Classification of Bacillus subtilis flagellins , 1977, Journal of bacteriology.

[8]  J. Slots.  The predominant cultivable microflora of advanced periodontitis. , 1977, Scandinavian journal of dental research.

[9]  J. Slots,et al.  Attachment of Bacteroides melaninogenicus subsp. asaccharolyticus to Oral Surfaces and Its Possible Role in Colonization of the Mouth and of Periodontal Pockets , 1978, Infection and immunity.

[10]  R. Genco,et al.  Direct hemagglutination technique for differentiating Bacteroides asaccharolyticus oral strains from nonoral strains , 1979, Journal of clinical microbiology.

[11]  S. Holt,et al.  Ultrastructure of Bacteroides species: Bacteroides asaccharolyticus, Bacteroides fragilis, Bacteroides melaninogenicus subspecies melaninogenicus, and B. melaninogenicus subspecies intermedius. , 1979, The Journal of infectious diseases.

[12]  G. Blobel,et al.  The four cytoplasmically made subunits of yeast mitochondrial cytochrome c oxidase are synthesized individually and not as a polyprotein. , 1980, Proceedings of the National Academy of Sciences of the United States of America.

[13]  J. Duguid,et al.  Adhesive Properties of Enterobacteriaceae , 1980 .

[14]  T. Buchanan,et al.  Structure and Cell Membrane-Binding Properties of Bacterial Fimbriae , 1980 .

[15]  B. Mansheim,et al.  Immunochemical differences between oral and nonoral strains of Bacteroides asaccharolyticus , 1980, Infection and immunity.

[16]  R. Genco,et al.  Antigenic studies of oral and nonoral black-pigmented Bacteroides strains. , 1980, Infection and immunity.

[17]  J. Dankert,et al.  Porin from the outer membrane of Escherichia coli: immunological characterization of native and heat-dissociated forms. , 1981, Journal of general microbiology.

[18]  R. Genco,et al.  Identification of Bacteroides gingivalis by fluorescent antibody staining. , 1981, Annales de microbiologie.

[19]  P. Klemm.  The complete amino-acid sequence of the K88 antigen, a fimbrial protein from Escherichia coli. , 2005, European journal of biochemistry.

[20]  P. Klemm.  Primary structure of the CFA1 fimbrial protein from human enterotoxigenic Escherichia coli strains. , 1982, European journal of biochemistry.

[21]  N. Mckern,et al.  Amino acid sequence of pilin from Bacteroides nodosus (strain 198), the causative organism of ovine footrot , 1983, FEBS letters.

[22]  Solubilization, isolation, and immunochemical characterization of the major outer membrane protein from Rhodopseudomonas sphaeroides. , 1983, The Journal of biological chemistry.

[23]  F. Yoshimura,et al.  Characterization of a trypsin-like protease from the bacterium Bacteroides gingivalis isolated from human dental plaque. , 1984, Archives of oral biology.