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Article ; Online: The Treponema denticola DgcA protein (TDE0125) is a functional diguanylate cyclase.

Patel, Dhara T / O'Bier, Nathaniel S / Schuler, Edward J A / Marconi, Richard T

Pathogens and disease

2021 Volume 79, Issue 3

Abstract: Periodontal disease (PD) is a progressive inflammatory condition characterized by degradation of the gingival epithelium, periodontal ligament, and alveolar bone ultimately resulting in tooth loss. Treponema denticola is a keystone periopathogen that ... ...

Abstract	Periodontal disease (PD) is a progressive inflammatory condition characterized by degradation of the gingival epithelium, periodontal ligament, and alveolar bone ultimately resulting in tooth loss. Treponema denticola is a keystone periopathogen that contributes to immune dysregulation and direct tissue destruction. As periodontal disease develops, T. denticola must adapt to environmental, immunological and physiochemical changes in the subgingival crevice. Treponema denticola produces bis-(3'-5')-cyclic dimeric guanosine monophosphate (c-di-GMP), an important regulatory nucleotide. While T. denticola encodes several putative diguanylate cyclases (DGCs), none have been studied and hence the biological role of c-di-GMP in oral treponemes remains largely unexplored. Here, we demonstrate that the T. denticola open reading frame, TDE0125, encodes a functional DGC designated as DgcA (Diguanylate cyclase A). The dgcA gene is universal among T. denticola isolates, highly conserved and is a stand-alone GGEEF protein with a GAF domain. Recombinant DgcA converts GTP to c-di-GMP using either manganese or magnesium under aerobic and anaerobic reaction conditions. Size exclusion chromatography revealed that DgcA exists as a homodimer and in larger oligomers. Site-directed mutagenesis of residues that define the putative inhibitory site of DgcA suggest that c-di-GMP production is allosterically regulated. This report is the first to characterize a DGC of an oral treponeme.
MeSH term(s)	Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Cyclic GMP/analogs & derivatives ; Cyclic GMP/metabolism ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Gene Expression Regulation, Bacterial ; Guanosine Triphosphate/metabolism ; Humans ; Mutagenesis, Site-Directed ; Periodontal Diseases/microbiology ; Phosphorus-Oxygen Lyases/genetics ; Phosphorus-Oxygen Lyases/metabolism ; Phylogeny ; Protein Domains ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Sequence Analysis, DNA ; Treponema denticola/enzymology ; Treponema denticola/physiology
Chemical Substances	Bacterial Proteins ; Escherichia coli Proteins ; Recombinant Proteins ; bis(3',5')-cyclic diguanylic acid (61093-23-0) ; Guanosine Triphosphate (86-01-1) ; Phosphorus-Oxygen Lyases (EC 4.6.-) ; diguanylate cyclase (EC 4.6.1.-) ; Cyclic GMP (H2D2X058MU)
Language	English
Publishing date	2021-01-15
Publishing country	United States
Document type	Journal Article
ISSN	2049-632X
ISSN (online)	2049-632X
DOI	10.1093/femspd/ftab004
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Article ; Online: Human and Veterinary Vaccines for Lyme Disease.

O'Bier, Nathaniel S / Hatke, Amanda L / Camire, Andrew C / Marconi, Richard T

Current issues in molecular biology

2020 Volume 42, Page(s) 191–222

Abstract: Lyme disease (LD) is an emerging zoonotic infection that is increasing in incidence in North America, Europe, and Asia. With the development of safe and efficacious vaccines, LD can potentially be prevented. Vaccination offers a cost-effective and safe ... ...

Abstract	Lyme disease (LD) is an emerging zoonotic infection that is increasing in incidence in North America, Europe, and Asia. With the development of safe and efficacious vaccines, LD can potentially be prevented. Vaccination offers a cost-effective and safe approach for decreasing the risk of infection. While LD vaccines have been widely used in veterinary medicine, they are not available as a preventive tool for humans. Central to the development of effective vaccines is an understanding of the enzootic cycle of LD, differential gene expression of
MeSH term(s)	Animals ; Borrelia burgdorferi/genetics ; Borrelia burgdorferi/immunology ; Disease Reservoirs/microbiology ; Disease Susceptibility ; Global Health ; Humans ; Lyme Disease/epidemiology ; Lyme Disease/microbiology ; Lyme Disease/prevention & control ; Lyme Disease/transmission ; Lyme Disease Vaccines/administration & dosage ; Lyme Disease Vaccines/immunology ; Population Surveillance ; Vaccination
Chemical Substances	Lyme Disease Vaccines
Language	English
Publishing date	2020-12-08
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2000024-8
ISSN	1467-3045 ; 1467-3037
ISSN (online)	1467-3045
ISSN	1467-3037
DOI	10.21775/cimb.042.191
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Article ; Online: Development of an FhbB based chimeric vaccinogen that elicits antibodies that block Factor H binding and cleavage by the periopathogen Treponema denticola.

O'Bier, Nathaniel S / Patel, Dhara T / Oliver, Lee D / Miller, Daniel P / Marconi, Richard T

Molecular oral microbiology

2020 Volume 36, Issue 1, Page(s) 50–57

Abstract: Treponema denticola is a proteolytic anaerobic spirochete and key contributor to periodontal disease of microbial etiology. As periodontal disease develops and progresses, T. denticola thrives in the hostile environment of the subgingival crevice by ... ...

Abstract	Treponema denticola is a proteolytic anaerobic spirochete and key contributor to periodontal disease of microbial etiology. As periodontal disease develops and progresses, T. denticola thrives in the hostile environment of the subgingival crevice by exploiting the negative regulatory activity of the complement protein, factor H (FH). FH bound to the cell surface receptor, FhbB (FH binding protein B), is competent to serve as a cofactor for the Factor I mediated-cleavage of the opsonin C3b. However, bound FH is ultimately cleaved by the T. denticola protease, dentilisin. As the T. denticola population expands, the rate of FH cleavage may exceed its rate of replenishment leading to local FH depletion and immune dysregulation culminating in tissue and ligament destruction and tooth loss. The goal of this study was to develop a T. denticola FhbB based-vaccine antigen that can block FH binding and cleavage and kill cells via antibody-mediated bactericidal activity. Tetra (FhbB-ch4) and pentavalent fhbB (FhbB-ch5) chimerics were engineered to have attenuated FH binding ability. The chimerics were immunogenic and elicited high-titer bactericidal and agglutinating antibody. Anti-Fhb-ch4 antisera blocked FH binding and cleavage by the T. denticola protease, dentilisin, in a dose dependent manner. Precedent for the use of FH binding proteins comes from the successful development of two FDA approved vaccines for type B Neiserria meningitidis. This study is the first to extend this approach to the development of a preventive or therapeutic vaccine (or monoclonal Ab) for periodontal disease.
MeSH term(s)	Bacterial Proteins/genetics ; Complement Factor H/genetics ; Peptide Hydrolases ; Treponema ; Treponema denticola ; Vaccines
Chemical Substances	Bacterial Proteins ; Vaccines ; Complement Factor H (80295-65-4) ; Peptide Hydrolases (EC 3.4.-)
Language	English
Publishing date	2020-12-09
Publishing country	Denmark
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2537726-7
ISSN	2041-1014 ; 2041-1006
ISSN (online)	2041-1014
ISSN	2041-1006
DOI	10.1111/omi.12325
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Article ; Online: FtlA and FtlB Are Candidates for Inclusion in a Next-Generation Multiantigen Subunit Vaccine for Lyme Disease.

Camire, Andrew C / O'Bier, Nathaniel S / Patel, Dhara T / Cramer, Nicholas A / Straubinger, Reinhard K / Breitschwerdt, Edward B / Funk, Rebecca A / Marconi, Richard T

Infection and immunity

2022 Volume 90, Issue 10, Page(s) e0036422

Abstract: Lyme disease (LD) is a tick-transmitted bacterial infection caused by Borreliella burgdorferi and other closely related species collectively referred to as the LD spirochetes. The LD spirochetes encode an uncharacterized family of proteins originally ... ...

Abstract	Lyme disease (LD) is a tick-transmitted bacterial infection caused by Borreliella burgdorferi and other closely related species collectively referred to as the LD spirochetes. The LD spirochetes encode an uncharacterized family of proteins originally designated
MeSH term(s)	Dogs ; Horses ; Animals ; Bacterial Outer Membrane Proteins/genetics ; Antibodies, Bacterial ; Lyme Disease/microbiology ; Borrelia burgdorferi ; Vaccines, Subunit/genetics ; Epitopes ; Lipoproteins/genetics ; Vaccines, Combined ; Immune Sera ; Frontotemporal Lobar Degeneration ; Ixodes/microbiology ; Antigens, Bacterial
Chemical Substances	Bacterial Outer Membrane Proteins ; Antibodies, Bacterial ; Vaccines, Subunit ; Epitopes ; Lipoproteins ; Vaccines, Combined ; Immune Sera ; Antigens, Bacterial
Language	English
Publishing date	2022-09-14
Publishing country	United States
Document type	Journal Article
ZDB-ID	218698-6
ISSN	1098-5522 ; 0019-9567
ISSN (online)	1098-5522
ISSN	0019-9567
DOI	10.1128/iai.00364-22
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Article ; Online: Antimicrobial activity of amixicile against Treponema denticola and other oral spirochetes associated with periodontal disease.

Reed, Lucas A / O'Bier, Nathaniel S / Oliver, Lee D / Hoffman, Paul S / Marconi, Richard T

Journal of periodontology

2018 Volume 89, Issue 12, Page(s) 1467–1474

Abstract: Background: Periodontal disease is a polymicrobial infection characterized by inflammation of the gingiva, alveolar bone resorption and tooth loss. As periodontal disease progresses, oral treponemes (spirochetes) become dominant bacteria in periodontal ... ...

Abstract	Background: Periodontal disease is a polymicrobial infection characterized by inflammation of the gingiva, alveolar bone resorption and tooth loss. As periodontal disease progresses, oral treponemes (spirochetes) become dominant bacteria in periodontal pockets. Oral treponemes are anaerobes and all encode the enzyme pyruvate-ferredoxin oxidoreductase (PFOR) which catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA. Here we assess the susceptibility of oral treponemes to amixicile (AMIX), a novel inhibitor of PFOR. Methods: The minimum inhibitory concentration (MIC) of AMIX against several oral treponeme species was determined. The impact of AMIX on processes relevant to virulence including motility, H Results: The growth of all oral treponeme species tested was inhibited by AMIX with MIC concentrations (MIC) ranging from 0.5-1.5 μg/mL. AMIX significantly reduced motility, caused a dose-dependent decrease in hydrogen sulfide production and increased sensitivity to killing by human complement (i.e., serum sensitivity). Conclusions: AMIX is effective in vitro in inhibiting growth and other processes central to virulence. AMIX could serve could serve as a new selective therapeutic tool for the treatment of periodontal disease.
MeSH term(s)	Anti-Infective Agents ; Benzamides ; Humans ; Periodontal Diseases ; Spirochaetales ; Thiazoles ; Treponema ; Treponema denticola
Chemical Substances	Anti-Infective Agents ; Benzamides ; Thiazoles ; amixicile
Language	English
Publishing date	2018-09-05
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	390921-9
ISSN	1943-3670 ; 0022-3492 ; 1049-8885 ; 0095-960X
ISSN (online)	1943-3670
ISSN	0022-3492 ; 1049-8885 ; 0095-960X
DOI	10.1002/JPER.17-0185
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Article: The

Ante, Vanessa M / Farris, Lauren C / Saputra, Elizabeth P / Hall, Allie J / O'Bier, Nathaniel S / Oliva Chávez, Adela S / Marconi, Richard T / Lybecker, Meghan C / Hyde, Jenny A

Frontiers in microbiology

2021 Volume 12, Page(s) 676192

Abstract: ... Borrelia ... ...

Abstract	Borrelia burgdorferi
Language	English
Publishing date	2021-05-25
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2587354-4
ISSN	1664-302X
ISSN	1664-302X
DOI	10.3389/fmicb.2021.676192
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Article: Development and optimization of OspC chimeritope vaccinogens for Lyme disease

Izac, Jerilyn R / O'Bier, Nathaniel S / Oliver, Lee D / Camire, Andrew C / Earnhart, Christopher G / LeBlanc Rhodes, DeLacy V / Young, Brandon F / Parnham, Stuart R / Davies, Christopher / Marconi, Richard T

Vaccine. 2020 Feb. 18, v. 38, no. 8

2020

Abstract: Experimental Outer surface protein (Osp) C based subunit chimeritope vaccinogens for Lyme disease (LD) were assessed for immunogenicity, structure, ability to elicit antibody (Ab) responses to divergent OspC proteins, and bactericidal activity. ... ...

Abstract	Experimental Outer surface protein (Osp) C based subunit chimeritope vaccinogens for Lyme disease (LD) were assessed for immunogenicity, structure, ability to elicit antibody (Ab) responses to divergent OspC proteins, and bactericidal activity. Chimeritopes are chimeric epitope based proteins that consist of linear epitopes derived from multiple proteins or multiple variants of a protein. An inherent advantage to chimeritope vaccinogens is that they can be constructed to trigger broadly protective Ab responses. Three OspC chimeritope proteins were comparatively assessed: Chv1, Chv2 and Chv3. The Chv proteins possess the same set of 18 linear epitopes derived from 9 OspC type proteins but differ in the physical ordering of epitopes or by the presence or absence of linkers. All Chv proteins were immunogenic in mice and rats eliciting high titer Ab. Immunoblot and enzyme linked immunosorbent assays demonstrated that the Chv proteins elicit IgG that recognizes a diverse array of OspC type proteins. The panel included OspC proteins produced by N. American and European strains of the LD spirochetes. Rat anti-Chv antisera uniformly labeled intact, non-permeabilized Borreliella burgdorferi demonstrating that vaccinal Ab can bind to targets that are naturally presented on the spirochete cell surface. Vaccinal Ab also displayed potent complement dependent-Ab mediated killing activity. This study highlights the ability of OspC chimeritopes to serve as vaccinogens that trigger potentially broadly protective Ab responses. In addition to the current use of an OspC chimeritope in a canine LD vaccine, chimeritopes can serve as key components of human LD subunit vaccines.
Keywords	Lyme disease ; Spirochaetes ; antibacterial properties ; antibodies ; antiserum ; complement ; dogs ; enzyme-linked immunosorbent assay ; epitopes ; humans ; immunogenicity ; immunoglobulin G ; subunit vaccines ; surface proteins
Language	English
Dates of publication	2020-0218
Size	p. 1915-1924.
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	605674-x
ISSN	1873-2518 ; 0264-410X
ISSN (online)	1873-2518
ISSN	0264-410X
DOI	10.1016/j.vaccine.2020.01.027
Database	NAL-Catalogue (AGRICOLA)

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Zs.MO 458: Show issues

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Article ; Online: Development and optimization of OspC chimeritope vaccinogens for Lyme disease.

Vaccine

2020 Volume 38, Issue 8, Page(s) 1915–1924

Abstract	Experimental Outer surface protein (Osp) C based subunit chimeritope vaccinogens for Lyme disease (LD) were assessed for immunogenicity, structure, ability to elicit antibody (Ab) responses to divergent OspC proteins, and bactericidal activity. Chimeritopes are chimeric epitope based proteins that consist of linear epitopes derived from multiple proteins or multiple variants of a protein. An inherent advantage to chimeritope vaccinogens is that they can be constructed to trigger broadly protective Ab responses. Three OspC chimeritope proteins were comparatively assessed: Chv1, Chv2 and Chv3. The Chv proteins possess the same set of 18 linear epitopes derived from 9 OspC type proteins but differ in the physical ordering of epitopes or by the presence or absence of linkers. All Chv proteins were immunogenic in mice and rats eliciting high titer Ab. Immunoblot and enzyme linked immunosorbent assays demonstrated that the Chv proteins elicit IgG that recognizes a diverse array of OspC type proteins. The panel included OspC proteins produced by N. American and European strains of the LD spirochetes. Rat anti-Chv antisera uniformly labeled intact, non-permeabilized Borreliella burgdorferi demonstrating that vaccinal Ab can bind to targets that are naturally presented on the spirochete cell surface. Vaccinal Ab also displayed potent complement dependent-Ab mediated killing activity. This study highlights the ability of OspC chimeritopes to serve as vaccinogens that trigger potentially broadly protective Ab responses. In addition to the current use of an OspC chimeritope in a canine LD vaccine, chimeritopes can serve as key components of human LD subunit vaccines.
MeSH term(s)	Animals ; Antibodies, Bacterial/immunology ; Antigens, Bacterial/immunology ; Bacterial Outer Membrane Proteins/immunology ; Borrelia burgdorferi/immunology ; Epitopes/immunology ; Lipoproteins/immunology ; Lyme Disease/prevention & control ; Lyme Disease Vaccines/immunology ; Mice ; Rats
Chemical Substances	Antibodies, Bacterial ; Antigens, Bacterial ; Bacterial Outer Membrane Proteins ; Epitopes ; Lipoproteins ; Lyme Disease Vaccines ; OspE protein, Borrelia burgdorferi
Language	English
Publishing date	2020-01-17
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	605674-x
ISSN	1873-2518 ; 0264-410X
ISSN (online)	1873-2518
ISSN	0264-410X
DOI	10.1016/j.vaccine.2020.01.027
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Article ; Online: Serologic Evidence for the Exposure of Eastern Coyotes (

Izac, Jerilyn R / Camire, Andrew C / Schuler, Edward J A / Hatke, Amanda L / O'Bier, Nathaniel S / Oliver, Lee D / Corondi, Avery / Plocinski, Olivia C / Desmond, Russell P / Naimi, Waheeda A / Carlyon, Jason A / Van Why, Kyle R / Shelly, Jennifer / Marconi, Richard T

mSphere

2020 Volume 5, Issue 4

Abstract: Lyme disease and anaplasmosis are tick-borne bacterial diseases caused ... ...

Abstract	Lyme disease and anaplasmosis are tick-borne bacterial diseases caused by
MeSH term(s)	Anaplasma phagocytophilum/genetics ; Animals ; Antibodies, Bacterial/blood ; Bacterial Proteins/genetics ; Bacterial Proteins/immunology ; Borrelia burgdorferi/genetics ; Coyotes/immunology ; Coyotes/microbiology ; Ehrlichiosis/epidemiology ; Ehrlichiosis/veterinary ; Female ; Ixodes/microbiology ; Lyme Disease/epidemiology ; Lyme Disease/veterinary ; Male ; Pennsylvania/epidemiology ; Serologic Tests ; Tick-Borne Diseases/epidemiology ; Tick-Borne Diseases/immunology ; Tick-Borne Diseases/veterinary
Chemical Substances	Antibodies, Bacterial ; Bacterial Proteins
Language	English
Publishing date	2020-08-12
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	2379-5042
ISSN (online)	2379-5042
DOI	10.1128/mSphere.00544-20
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Article ; Online: The Treponema denticola FhbB Protein Is a Dominant Early Antigen That Elicits FhbB Variant-Specific Antibodies That Block Factor H Binding and Cleavage by Dentilisin.

Miller, Daniel P / Oliver, Lee D / Tegels, Brittney K / Reed, Lucas A / O'Bier, Nathaniel S / Kurniyati, Kurni / Faust, Lindsay A / Lawson, Christine K / Allard, Anna M / Caimano, Melissa J / Marconi, Richard T

Infection and immunity

2016 Volume 84, Issue 7, Page(s) 2051–2058

Abstract: The Treponema denticola FhbB protein contributes to immune evasion by binding factor H (FH). Cleavage of FH by the T. denticola protease, dentilisin, may contribute to the local immune dysregulation that is characteristic of periodontal disease (PD). ... ...

Abstract	The Treponema denticola FhbB protein contributes to immune evasion by binding factor H (FH). Cleavage of FH by the T. denticola protease, dentilisin, may contribute to the local immune dysregulation that is characteristic of periodontal disease (PD). Although three FhbB phyletic types have been defined (FhbB1, FhbB2, and FhbB3), the in vivo expression patterns and antigenic heterogeneity of FhbB have not been assessed. Here, we demonstrate that FhbB is a dominant early antigen that elicits FhbB type-specific antibody (Ab) responses. Using the murine skin abscess model, we demonstrate that the presence or absence of FhbB or dentilisin significantly influences Ab responses to infection and skin abscess formation. Competitive binding analyses revealed that α-FhbB Ab can compete with FH for binding to T. denticola and block dentilisin-mediated FH cleavage. Lastly, we demonstrate that dentilisin cleavage sites reside within critical functional domains of FH, including the complement regulatory domain formed by CCPs 1 to 4. Analysis of the FH cleavage products revealed that they lack cofactor activity. The data presented here provide insight into the in vivo significance of dentilisin, FhbB and its antigenic diversity, and the potential impact of FH cleavage on the regulation of complement activation.
MeSH term(s)	Animals ; Antibodies, Bacterial/immunology ; Antibodies, Monoclonal/immunology ; Antibodies, Monoclonal/pharmacology ; Antibody Specificity/immunology ; Antigens, Bacterial/immunology ; Antigens, Bacterial/metabolism ; Bacterial Proteins/immunology ; Bacterial Proteins/metabolism ; Binding, Competitive ; Complement Factor H/chemistry ; Complement Factor H/immunology ; Complement Factor H/metabolism ; Mice ; Peptide Hydrolases/metabolism ; Protein Binding/drug effects ; Protein Binding/immunology ; Protein Interaction Domains and Motifs ; Proteolysis ; Treponema denticola/immunology
Chemical Substances	Antibodies, Bacterial ; Antibodies, Monoclonal ; Antigens, Bacterial ; Bacterial Proteins ; Complement Factor H (80295-65-4) ; Peptide Hydrolases (EC 3.4.-) ; dentilisin (EC 3.4.21.-)
Language	English
Publishing date	2016-06-23
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	218698-6
ISSN	1098-5522 ; 0019-9567
ISSN (online)	1098-5522
ISSN	0019-9567
DOI	10.1128/IAI.01542-15
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