PubMed Health⌕ Search

PubMed · 1821458

Fc-binding components: a virulence factor in Actinobacillus actinomycetemcomitans?

Abstract

Actinobacillus actinomycetemcomitans (ATCC 33384) can produce and release components that bind to the Fc part of IgG. Fc-binding components were observed in whole bacteria, capsular material and medium from broth cultures. The components were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoblotted with biotinylated Fc-fragments and myeloma proteins. In a phagocytosis assay with human granulocytes and sheep erythrocytes, preincubation of opsonized erythrocytes with protein A reduced phagocytosis by 90%. In contrast, preincubation of the opsonizing antibody with medium components from a culture of A. actinomycetemcomitans enhanced the opsonizing effect of the antibody. The enhanced binding of erythrocytes may be caused by formation of aggregates between opsonizing antibody and bacterial Fc-binding components. Aggregated IgG can bind to low-affinity Fc gamma II and gamma III receptors that cannot bind monomeric IgG. Release of Fc-binding components from bacteria may contribute to the periodontal lesion through interference with the phagocytic activity of granulocytes and with the complement system. Fc-binding components may also interfere with downregulation of the B-cell response.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

K Tolo, K Helgeland. 1991. Fc-binding components: a virulence factor in Actinobacillus actinomycetemcomitans?. https://doi.org/10.1111/j.1399-302x.1991.tb00509.x

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Elevated IgG titers to periodontal pathogens related to Buerger disease.

BACKGROUND: Periodontal pathogens were frequently detected in the occluded arteries of Buerger disease patients, hence we hypothesized that the infection from periodontal pathogens may be associated with Buerger disease. METHODS: We investigated periodontal status using various clinical parameters and serum IgG antibody levels against T. denticola, P. gingivalis, A. actinomycetemcomitans and P. intermedia in nineteen Buerger disease patients and fifteen control subjects. The results were statistically analyzed. RESULTS: The prevalence of periodontitis and the percentages of probing sites with PD> or =4 mm and CAL> or =4 mm were significantly higher in the patient group (P<0.001, P=0.016, and P<0.001, respectively). Patients had significantly higher serum IgG titers against T. denticola, P. gingivalis and A. actinomycetemcomitans (P=0.002, P=0.039, and P=0.011, respectively). CONCLUSIONS: This study provides evidence for possible implications of periodontitis in Buerger disease.

Aggregatibacter actinomycetemcomitans↗

Iron acquisition in the dental pathogen Actinobacillus actinomycetemcomitans: what does it use as a source and how does it get this essential metal?

Actinobacillus actinomycetemcomitans requires iron to grow under limiting conditions imposed by synthetic and natural chelators. Although none of the strains tested used hemoglobin, lactoferrin or transferrin, all of them used FeCl3 and hemin as iron sources under chelated conditions. Dot-blot binding assays showed that all strains bind lactoferrin, hemoglobin, and hemin but not transferrin. When compared with smooth strains, the rough isolates showed higher hemin binding activity, which was sensitive to proteinase K treatment. A. actinomycetemcomitans harbors the Fur-regulated afeABCD locus coding for iron acquisition in isogenic and non-isogenic cell backgrounds. The genome of this oral pathogen also harbors several other predicted iron uptake genes including the hitABC locus, which restored iron acquisition in the E. coli 1017 ent mutant. However, the disruption of this locus in the parental strain did not affect iron acquisition as drastically as the inactivation of AfeABCD, suggesting that the latter system could be more involved in iron transport than the HitABC system. The genome of this oral pathogen also harbors an active copy of the exbBexbDtonB operon, which could provide the energy needed for hemin acquisition. However, inactivation of each coding region of this operon did not affect the hemin and iron acquisition phenotypes of isogenic derivatives. This observation suggests that the function of these proteins could be replaced by those coded for by tolQ, tolR and tolA as it was described for other bacterial transport systems. Interruption of a hasR homolog, an actively transcribed gene that is predicted to code for an outer membrane hemophore receptor protein, did not affect the ability of an isogenic derivative to bind and use hemin under chelated conditions. This result also indicates that A. actinomycetemcomitans could produce more than one outer membrane hemin receptor as it was described in other human pathogens. All strains tested formed biofilms on plastic under iron-rich and iron-chelated conditions. However, smooth strains attached poorly and formed weaker biofilms when compared with rough isolates. The incubation of rough cells in the presence of FeCl3 or hemin resulted in an increased number of smaller aggregates and microcolonies as compared to the fewer but larger aggregates formed when cells were grown in the presence of dipyridyl.

Aggregatibacter actinomycetemcomitans↗