scholarly journals Antioxidant effect of minocycline in gingival epithelium induced by Actinobacillus actinomycetemcomitans serotype B toxin

2009 ◽  
Vol 42 (1) ◽  
pp. 41
Author(s):  
Ernie Maduratna Setiawati
Keyword(s):  
Antioxidant Effect ◽  
Actinobacillus Actinomycetemcomitans ◽  
Gingival Epithelium ◽  
Serotype B

scholarly journals Cloning of the Gene Encoding the Actinobacillus actinomycetemcomitans Serotype b OmpA-Like Outer Membrane Protein

1999 ◽  
Vol 67 (2) ◽  
pp. 942-945 ◽  
Author(s):  
Hitoshi Komatsuzawa ◽  
Toshihisa Kawai ◽  
Mark E. Wilson ◽  
Martin A. Taubman ◽  
Motoyuki Sugai ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Amino Acid ◽  
Membrane Protein ◽  
Amino Acid Sequence ◽  
Molecular Mass ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Actinobacillus Actinomycetemcomitans ◽  
Gene Encoding ◽  
Serotype B

ABSTRACT The gene encoding an outer membrane protein A (OmpA)-like, heat-modifiable Omp of Actinobacillus actinomycetemcomitans ATCC 43718 (strain Y4, serotype b) was cloned by a PCR cloning procedure. DNA sequence analysis revealed that the gene encodes a protein of 346 amino acid residues with a molecular mass of 36.9 kDa. The protein expressed by the cloned gene reacted with a monoclonal antibody to the previously described 29-kDa Omp (Omp29) of strain Y4. This monoclonal antibody reacted specifically with Omp29 of A. actinomycetemcomitans (serotype b), but not with any Omp of Escherichia coli, including OmpA. This protein exhibited characteristic heat modifiability on sodium dodecyl sulfate-polyacrylamide gels, showing an apparent molecular mass of 29 kDa when unheated and a mass of 34 kDa when heated. The N-terminal amino acid sequence of the protein expressed inE. coli perfectly matched those deduced from the purified Omp29 of strain Y4. The deduced amino acid sequence of the gene coding for Omp29 from serotype b matched completely (except for valine at position 321) that of a recently reported omp34gene described for A. actinomycetemcomitans serotype c (NCTC 9710). Because of the conserved nature of the gene within these serotypes, we designated the gene described herein from serotype b asomp34.

scholarly journals Structural and Genetic Analyses of O Polysaccharide from Actinobacillus actinomycetemcomitans Serotype f

2001 ◽  
Vol 69 (9) ◽  
pp. 5375-5384 ◽  
Author(s):  
Jeffrey B. Kaplan ◽  
Malcolm B. Perry ◽  
Leann L. MacLean ◽  
David Furgang ◽  
Mark E. Wilson ◽  
...  
Keyword(s):  
Gene Cluster ◽  
Gene Clusters ◽  
Pcr Primers ◽  
Cross Reactivity ◽  
Actinobacillus Actinomycetemcomitans ◽  
Molar Ratio ◽  
African American Female ◽  
Specific Pcr ◽  
Serotype B ◽  
Transposon Insertions

ABSTRACT The oral bacterium Actinobacillus actinomycetemcomitans is implicated as a causative agent of localized juvenile periodontitis (LJP). A. actinomycetemcomitans is classified into five serotypes (a to e) corresponding to five structurally and antigenically distinct O polysaccharide (O-PS) components of their respective lipopolysaccharide molecules. Serotype b has been reported to be the dominant serotype isolated from LJP patients. We determined the lipopolysaccharide O-PS structure from A. actinomycetemcomitans CU1000, a strain isolated from a 13-year-old African-American female with LJP which had previously been classified as serotype b. The O-PS of strain CU1000 consisted of a trisaccharide repeating unit composed ofl-rhamnose and 2-acetamido-2-deoxy-d-galactose (molar ratio, 2:1) with the structure →2)-α-l-Rhap-(1–3)-2-O-(β-d-GalpNAc)-α-l-Rhap-(1→. O-PS from strain CU1000 was structurally and antigenically distinct from the O-PS molecules of the five known A. actinomycetemcomitans serotypes. Strain CU1000 was mutagenized with transposon IS903φkan, and three mutants that were deficient in O-PS synthesis were isolated. All three transposon insertions mapped to a single 1-kb region on the chromosome. The DNA sequence of a 13.1-kb region surrounding these transposon insertions contained a cluster of 14 open reading frames that was homologous to gene clusters responsible for the synthesis of A. actinomycetemcomitans serotype b, c, and e O-PS antigens. The CU1000 gene cluster contained two genes that were not present in serotype-specific O-PS antigen clusters of the other five knownA. actinomycetemcomitans serotypes. These data indicate that strain CU1000 should be assigned to a new A. actinomycetemcomitans serotype, designated serotype f. A PCR assay using serotype-specific PCR primers showed that 3 out of 20 LJP patients surveyed (15%) harbored A. actinomycetemcomitans strains carrying the serotype f gene cluster. The finding of an A. actinomycetemcomitansserotype showing serological cross-reactivity with anti-serotype b-specific antiserum suggests that a reevaluation of strains previously classified as serotype b may be warranted.

scholarly journals Novel Apoptosis-Inducing Activity inBacteroides forsythus: a Comparative Study with Three Serotypes of Actinobacillus actinomycetemcomitans

2000 ◽  
Vol 68 (8) ◽  
pp. 4611-4615 ◽  
Author(s):  
Shinichi Arakawa ◽  
Takuma Nakajima ◽  
Hiroaki Ishikura ◽  
Shizuko Ichinose ◽  
Isao Ishikawa ◽  
...  
Keyword(s):  
Caspase 3 ◽  
Apoptotic Cell ◽  
White Blood Cells ◽  
Membrane Integrity ◽  
Cytolytic Activity ◽  
Actinobacillus Actinomycetemcomitans ◽  
Leukemic Cells ◽  
Dna Ladder ◽  
Serotype A ◽  
Serotype B

ABSTRACT Bacteroides forsythus, which has been reported to be associated with periodontitis but has not been recognized as a key pathogen, was found to induce cytolytic activity against HL-60 and other human leukemic cells. This cytolytic activity was demonstrated according to three different criteria: (i) loss of both mitochondrial membrane potential and membrane integrity in cells treated with bacterial extracts and then with Rh123 and propidium iodide, respectively, as demonstrated by flow cytometry; (ii) damage to cytoplasmic membrane, as revealed by scanning electron microscopy (SEM); and (iii) DNA ladder formation and activation of caspase-3. These results indicate that B. forsythus produced an apoptosis-inducing factor(s) found to be composed of protein as judged by heat and trypsin sensitivity. In addition to extracts from B. forsythus, the culture supernatant of this bacterium has the ability to induce a cytolytic effect against peripheral white blood cells, especially lymphocytes. For comparison with B. forsythus, the same analyses were applied to two strains with different serotypes ofActinobacillus actinomycetemcomitans, serotypes a (ATCC 43717) and c (ATCC 43719), in addition to previously reported apoptosis-inducing serotype b (ATCC 43718), which was used as a positive control. The strains of A. actinomycetemcomitansserotypes a and b induced apoptosis in HL-60 cells as judged by the above three criteria but to a slightly lesser extent than did B. forsythus, while the serotype c strain produced apoptosis to a negligible extent. Detailed SEM images showed that the A. actinomycetemcomitans serotype a strain induced large-pore formation and the serotype b strain produced small pores with typical blebbing, while B. forsythus induced severe membrane ruffling. Further DNA ladder formation and caspase-3 activation were observed in the serotype a and b strains but not in the serotype c strain. The present paper is the first report of a protein factor(s) from B. forsythus and the A. actinomycetemcomitans serotype a strain which induces apoptotic cell death.

scholarly journals Molecular Cloning of the fur Gene from Actinobacillus actinomycetemcomitans

2002 ◽  
Vol 70 (6) ◽  
pp. 3170-3179 ◽  
Author(s):  
V. I. Haraszthy ◽  
E. T. Lally ◽  
G. G. Haraszthy ◽  
J. J. Zambon
Keyword(s):  
Gene Product ◽  
Bacterial Species ◽  
Consensus Sequence ◽  
Actinobacillus Actinomycetemcomitans ◽  
Gene Probe ◽  
Virulence Determinants ◽  
Chromosomal Dna ◽  
E Coli ◽  
Therapeutic Modalities ◽  
Serotype B

ABSTRACT In several bacterial species, iron availability in host tissues is coordinated with the expression of virulence determinants through the fur gene product. Initial experiments showed that a cloned Escherichia coli fur gene probe hybridized to Southern blots of Actinobacillus actinomycetemcomitans strain JP2 (serotype b) chromosomal DNA. The A. actinomycetemcomitans fur gene was then cloned utilizing partial functional complementation of the fur mutant in E. coli strain H1780. Analysis of the cloned DNA sequence revealed a 438-bp open reading frame with a deduced 146-amino-acid sequence exhibiting 80% identity to Haemophilus influenzae Fur and 62% identity to E. coli Fur. The pUC Aafur gene probe (generated from JP2 serotype b) hybridized to representatives from all five A. actinomycetemcomitans serotypes as well as to two strains derived from monkeys, suggesting that fur is widely distributed in A. actinomycetemcomitans. Open reading frames having >70% identity with the E. coli and H. influenzae flavodoxin and gyrase A genes, respectively, were found. Expression of the A. actinomycetemcomitans fur gene product repressed fiu expression and siderophore production in E. coli. A gel shift assay demonstrated that the expressed A. actinomycetemcomitans Fur protein bound the bacterial fur consensus sequence. Further characterization of the fur gene product in A. actinomycetemcomitans may improve our understanding of its role in the pathogenesis of periodontal disease and may lead to specific therapeutic modalities.

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