Structure of Factor H-binding Protein B (FhbB) of the Periopathogen, Treponema denticola

Miller, Daniel P.; Bell, Jessica K.; McDowell, John V.; Conrad, Daniel H.; Burgner, John W.; Héroux, A.; Marconi, Richard T.

doi:10.1074/jbc.m112.339721

Cited by 40 publications

(91 citation statements)

References 54 publications

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“…Gingipains, surface polysaccharides, and C4BP-binding proteins in P. gingivalis have been characterized in previous studies (32,33). In T. denticola, FhbB has been reported to have factor H-binding activity (44). In the present study, we demonstrated that the S-layer was involved in serum resistance.…”

Section: Discussionsupporting

confidence: 62%

The Surface Layer of Tannerella forsythia Contributes to Serum Resistance and Oral Bacterial Coaggregation

et al. 2013

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e Tannerella forsythia is an anaerobic, Gram-negative bacterium involved in the so-called "red complex," which is associated with severe and chronic periodontitis. The surface layer (S-layer) of T. forsythia is composed of cell surface glycoproteins, such as TfsA and TfsB, and is known to play a role in adhesion/invasion and suppression of proinflammatory cytokine expression. Here we investigated the association of this S-layer with serum resistance and coaggregation with other oral bacteria. The growth of the S-layer-deficient mutant in a bacterial medium containing more than 20% non-heat-inactivated calf serum (CS) or more than 40% non-heat-inactivated human serum was significantly suppressed relative to that of the wild type (WT). Next, we used confocal microscopy to perform quantitative analysis on the effect of serum. The survival ratio of the mutant exposed to 100% non-heat-inactivated CS (76% survival) was significantly lower than that of the WT (97% survival). Furthermore, significant C3b deposition was observed in the mutant but not in the WT. In a coaggregation assay, the mutant showed reduced coaggregation with Streptococcus sanguinis, Streptococcus salivarius, and Porphyromonas gingivalis but strong coaggregation with Fusobacterium nucleatum. These results indicated that the S-layer of T. forsythia plays multiple roles in virulence and may be associated with periodontitis.

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Section: Discussionsupporting

confidence: 62%

The Surface Layer of Tannerella forsythia Contributes to Serum Resistance and Oral Bacterial Coaggregation

et al. 2013

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“…Our recent surface charge distribution analysis indicated that the Fhb II surface is rich in amino acids with both negative and positive charges (25), which may contribute to the electrostatic interactions between Fhb and FH/C3. Previous studies have shown that FhbB and Fhbp bound to human FH mainly through surface-exposed negatively charged amino acids (21,29). However, Efb bound to C3 through positively charged amino acids on the Efb protein (24).…”

Section: Discussionmentioning

confidence: 96%

Mechanisms of Host-Pathogen Protein Complex Formation and Bacterial Immune Evasion of Streptococcus suis Protein Fhb

Liu

Gan

Zhang

et al. 2016

Journal of Biological Chemistry

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“…Investigations at the structural level might provide indications on the nature of the detailed FH/PH interaction. At present, only one protein interacting with , that is, B. burgdorferi OspE has been determined at the structural level, whereas the structures of three proteins, which bind to SCRs 6-7, have been revealed in detail (59)(60)(61)(62). Interestingly, no structural resemblance was established between these microbial proteins.…”

Section: Discussionmentioning

confidence: 99%

Identification of a Haemophilus influenzae Factor H–Binding Lipoprotein Involved in Serum Resistance

Fleury

Hallström

et al. 2014

The Journal of Immunology

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Haemophilus influenzae is a Gram-negative human pathogen that resides in the upper respiratory tract. Encapsulated H. influenzae type b (Hib) and type f (Hif) are the most common serotypes associated with invasive disease. H. influenzae displays various strategies to circumvent the host innate immune response, including the bactericidal effect of the complement system. In this study, we identified an H. influenzae lipoprotein having the ability to bind factor H (FH), the major regulator of the alternative pathway of complement activation. This protein, named protein H (PH), was surface exposed and was found in all clinical Hib and Hif isolates tested. Deletion of the gene encoding for PH (lph) in Hib and Hif significantly reduced the interaction between bacteria and FH. When Hib and Hif PH variants were separately expressed in nontypeable (unencapsulated) H. influenzae, which did not bind FH, an increased FH affinity was observed. We recombinantly expressed the two PH variants in Escherichia coli, and despite sharing only 56% identical amino acids, both FH-binding Haemophilus proteins similarly interacted with the complement regulator FH short consensus repeats 7 and 18–20. Importantly, Hib and Hif resistance against the bactericidal effect of human serum was significantly reduced when bacterial mutants devoid of PH were tested. In conclusion, we have characterized a hitherto unknown bacterial protein that is crucial for mediating an interaction between the human pathogen H. influenzae and FH. This novel interaction is important for H. influenzae resistance against complement activation and will consequently promote bacterial pathogenesis.

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Structure of Factor H-binding Protein B (FhbB) of the Periopathogen, Treponema denticola

Cited by 40 publications

References 54 publications

The Surface Layer of Tannerella forsythia Contributes to Serum Resistance and Oral Bacterial Coaggregation

The Surface Layer of Tannerella forsythia Contributes to Serum Resistance and Oral Bacterial Coaggregation

Mechanisms of Host-Pathogen Protein Complex Formation and Bacterial Immune Evasion of Streptococcus suis Protein Fhb

Identification of a Haemophilus influenzae Factor H–Binding Lipoprotein Involved in Serum Resistance

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