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Article ; Online: Pros and cons of causative association between periodontitis and rheumatoid arthritis.

Koziel, Joanna / Potempa, Jan

Periodontology 2000

2022 Volume 89, Issue 1, Page(s) 83–98

Abstract: Research in recent decades has brought significant advancements in understanding of the molecular basis of the etiology of autoimmune diseases, including rheumatoid arthritis, a common systemic disease in which an inappropriate or inadequate immune ... ...

Abstract	Research in recent decades has brought significant advancements in understanding of the molecular basis of the etiology of autoimmune diseases, including rheumatoid arthritis, a common systemic disease in which an inappropriate or inadequate immune response to environmental challenges leads to joint destruction. Recent studies have indicated that the classical viewpoint of the immunological processes underpinning the pathobiology of rheumatoid arthritis is restricted and needs to be expanded to include a more holistic and interdisciplinary approach incorporating bacteria-induced inflammatory reactions as an important pathway in rheumatoid arthritis etiology. Here, we discuss in detail data showing the clinical and molecular association of rheumatoid arthritis development with periodontal diseases. We also describe the unique role of periopathogens, which have been proposed to be crucial in the initiation and progression of this autoimmune pathological disorder.
MeSH term(s)	Arthritis, Rheumatoid/complications ; Autoimmune Diseases ; Humans ; Inflammation ; Periodontal Diseases ; Periodontitis/complications
Language	English
Publishing date	2022-03-09
Publishing country	Denmark
Document type	Journal Article ; Review ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1200504-6
ISSN	1600-0757 ; 0906-6713
ISSN (online)	1600-0757
ISSN	0906-6713
DOI	10.1111/prd.12432
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Article ; Online: Dying for a cause: The pathogenic manipulation of cell death and efferocytic pathways.

Cooper, Kelley N / Potempa, Jan / Bagaitkar, Juhi

Molecular oral microbiology

2023

Abstract: Cell death is a natural consequence of infection. However, although the induction of cell death was solely thought to benefit the pathogen, compelling data now show that the activation of cell death pathways serves as a nuanced antimicrobial strategy ... ...

Abstract	Cell death is a natural consequence of infection. However, although the induction of cell death was solely thought to benefit the pathogen, compelling data now show that the activation of cell death pathways serves as a nuanced antimicrobial strategy that couples pathogen elimination with the generation of inflammatory cytokines and the priming of innate and adaptive cellular immunity. Following cell death, the phagocytic uptake of the infected dead cell by antigen-presenting cells and the subsequent lysosomal fusion of the apoptotic body containing the pathogen serve as an important antimicrobial mechanism that furthers the development of downstream adaptive immune responses. Despite the complexity of regulated cell death pathways, pathogens are highly adept at evading them. Here, we provide an overview of the remarkable diversity of cell death and efferocytic pathways and discuss illustrative examples of virulence strategies employed by pathogens, including oral pathogens, to counter their activation and persist within the host.
Language	English
Publishing date	2023-10-02
Publishing country	Denmark
Document type	Journal Article ; Review
ZDB-ID	2537726-7
ISSN	2041-1014 ; 2041-1006
ISSN (online)	2041-1014
ISSN	2041-1006
DOI	10.1111/omi.12436
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Zs.A 2199: Show issues

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Article ; Online: Phage display selection of human single domain antibodies towards karilysin, a metalloproteinase and secreted virulence factor from Tannerella forsythia.

Skottrup, Peter Durand / Książek, Mirosław / Potempa, Jan

Journal of immunological methods

2023 Volume 516, Page(s) 113458

Abstract: Metalloproteases derived from microbial pathogens are important virulence factors contributing to evasion of antimicrobial mechanisms of the innate immune system. Karilysin is a metalloprotease recently discovered in the periodonto-pathogen Tanneralla ... ...

Abstract	Metalloproteases derived from microbial pathogens are important virulence factors contributing to evasion of antimicrobial mechanisms of the innate immune system. Karilysin is a metalloprotease recently discovered in the periodonto-pathogen Tanneralla forsythia and currently no monoclonal antibodies exist against karilysin, which is a gap in the molecular toolbox for structure-function studies of karilysin. In this study we have used phage display for fast selection of single domain antibodies (VHs) towards the karilysin catalytic domain (Kly18) using a human domain library based on a VH framework. Following five panning rounds, phage clones were sequenced, and three unique sequences were identified (termed Kly18-VHI-III). Initial screens identified Kly18-VHII-phage as capable of inhibiting Kly18 proteolytic activity. The free Kly18-VHII was expressed in the periplasmic space of BL21 E. coli using the pET22b (+) vector and purified by IMAC and the inhibition capacity of purified Kly18-VHII was confirmed. The data presented in this study provides input to the molecular toolbox for the study of karilysin and Kly18-VHII could serve as a lead molecule for development of a karilysin-specific inhibitor.
MeSH term(s)	Humans ; Tannerella forsythia ; Virulence Factors/genetics ; Single-Domain Antibodies/genetics ; Matrix Metalloproteinases ; Escherichia coli ; Bacteriophages/genetics ; Peptide Library
Chemical Substances	Virulence Factors ; Single-Domain Antibodies ; Matrix Metalloproteinases (EC 3.4.24.-) ; Peptide Library
Language	English
Publishing date	2023-03-14
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	120142-6
ISSN	1872-7905 ; 0022-1759
ISSN (online)	1872-7905
ISSN	0022-1759
DOI	10.1016/j.jim.2023.113458
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Article ; Online: Phage display selection of human single domain antibodies towards karilysin, a metalloproteinase and secreted virulence factor from Tannerella forsythia

Skottrup, Peter Durand / Książek, Mirosław / Potempa, Jan

Journal of Immunological Methods. 2023 May, v. 516 p.113458-

2023

Abstract	Metalloproteases derived from microbial pathogens are important virulence factors contributing to evasion of antimicrobial mechanisms of the innate immune system. Karilysin is a metalloprotease recently discovered in the periodonto-pathogen Tanneralla forsythia and currently no monoclonal antibodies exist against karilysin, which is a gap in the molecular toolbox for structure-function studies of karilysin. In this study we have used phage display for fast selection of single domain antibodies (VHs) towards the karilysin catalytic domain (Kly18) using a human domain library based on a VH framework. Following five panning rounds, phage clones were sequenced, and three unique sequences were identified (termed Kly18-VHI-III). Initial screens identified Kly18-VHII-phage as capable of inhibiting Kly18 proteolytic activity. The free Kly18-VHII was expressed in the periplasmic space of BL21 E. coli using the pET22b (+) vector and purified by IMAC and the inhibition capacity of purified Kly18-VHII was confirmed. The data presented in this study provides input to the molecular toolbox for the study of karilysin and Kly18-VHII could serve as a lead molecule for development of a karilysin-specific inhibitor.
Keywords	Bacteroides forsythus ; Escherichia coli ; active sites ; bacteriophages ; humans ; innate immunity ; metalloproteinases ; peptide libraries ; proteolysis ; virulence ; Phage display ; Karilysin ; Single domain antibody ; Metalloproteinase
Language	English
Dates of publication	2023-05
Publishing place	Elsevier B.V.
Document type	Article ; Online
ZDB-ID	120142-6
ISSN	1872-7905 ; 0022-1759
ISSN (online)	1872-7905
ISSN	0022-1759
DOI	10.1016/j.jim.2023.113458
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Article ; Online: Screening and characterization of aptamers recognizing the periodontal pathogen Tannerella forsythia.

Mizgalska, Danuta / Malicki, Stanisław / Golda, Anna / Chruścicka-Smaga, Barbara / Potempa, Jan

FEBS open bio

2024 Volume 14, Issue 3, Page(s) 498–504

Abstract: Periodontal disease is one of the most common forms of inflammation. It is currently diagnosed by observing symptoms such as gingival bleeding and attachment loss. However, the detection of biomarkers that precede such symptoms would allow earlier ... ...

Abstract	Periodontal disease is one of the most common forms of inflammation. It is currently diagnosed by observing symptoms such as gingival bleeding and attachment loss. However, the detection of biomarkers that precede such symptoms would allow earlier diagnosis and prevention. Aptamers are short oligonucleotides or peptides that fold into three-dimensional conformations conferring the ability to bind molecular targets with high affinity and specificity. Here we report the selection of aptamers that bind specifically to the bacterium Tannerella forsythia, a pathogen frequently associated with periodontal disease. Two aptamers with the highest affinity were examined in more detail, revealing that their binding is probably dependent on mirolysin, a surface-associated protease secreted by the T. forsythia type-9 secretion system. The aptamers showed minimal cross-reactivity to other periodontopathogens and are therefore promising leads for the development of new tools to study the composition of the periodontitis-associated dysbiotic bacteriome as well as inexpensive new diagnostic assays.
MeSH term(s)	Humans ; Tannerella forsythia ; Periodontitis/diagnosis ; Periodontitis/microbiology ; Inflammation ; Peptide Hydrolases ; Oligonucleotides
Chemical Substances	Peptide Hydrolases (EC 3.4.-) ; Oligonucleotides
Language	English
Publishing date	2024-02-02
Publishing country	England
Document type	Journal Article
ZDB-ID	2651702-4
ISSN	2211-5463 ; 2211-5463
ISSN (online)	2211-5463
ISSN	2211-5463
DOI	10.1002/2211-5463.13772
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Article ; Online: The subversion of toll-like receptor signaling by bacterial and viral proteases during the development of infectious diseases.

Ciaston, Izabela / Dobosz, Ewelina / Potempa, Jan / Koziel, Joanna

Molecular aspects of medicine

2022 Volume 88, Page(s) 101143

Abstract: Toll-like receptors (TLRs) are pattern recognition receptors (PRRs) that respond to pathogen-associated molecular patterns (PAMPs). The recognition of specific microbial ligands by TLRs triggers an innate immune response and also promotes adaptive ... ...

Abstract	Toll-like receptors (TLRs) are pattern recognition receptors (PRRs) that respond to pathogen-associated molecular patterns (PAMPs). The recognition of specific microbial ligands by TLRs triggers an innate immune response and also promotes adaptive immunity, which is necessary for the efficient elimination of invading pathogens. Successful pathogens have therefore evolved strategies to subvert and/or manipulate TLR signaling. Both the impairment and uncontrolled activation of TLR signaling can harm the host, causing tissue destruction and allowing pathogens to proliferate, thus favoring disease progression. In this context, microbial proteases are key virulence factors that modify components of the TLR signaling pathway. In this review, we discuss the role of bacterial and viral proteases in the manipulation of TLR signaling, highlighting the importance of these enzymes during the development of infectious diseases.
MeSH term(s)	Humans ; Communicable Diseases/metabolism ; Communicable Diseases/microbiology ; Immunity, Innate ; Signal Transduction ; Toll-Like Receptors/genetics ; Toll-Like Receptors/metabolism ; Viral Proteases/immunology ; Viral Proteases/metabolism ; Bacterial Proteins/immunology ; Bacterial Proteins/metabolism ; Peptide Hydrolases/immunology ; Peptide Hydrolases/metabolism ; Virus Diseases/metabolism ; Bacterial Infections/metabolism
Chemical Substances	Toll-Like Receptors ; Viral Proteases (EC 3.4.-) ; Bacterial Proteins ; Peptide Hydrolases (EC 3.4.-)
Language	English
Publishing date	2022-09-21
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	197640-0
ISSN	1872-9452 ; 0098-2997
ISSN (online)	1872-9452
ISSN	0098-2997
DOI	10.1016/j.mam.2022.101143
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Zs.A 1189: Show issues

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Article ; Online: Complement Activation as a Helping Hand for Inflammophilic Pathogens and Cancer.

Okrój, Marcin / Potempa, Jan

Frontiers in immunology

2019 Volume 9, Page(s) 3125

Abstract: The complement system, an evolutionarily ancient component of innate immunity, is capable of protecting hosts from invading pathogens, either directly, by lysis of target cells, or indirectly, by mobilization of host immune mechanisms. However, this ... ...

Abstract	The complement system, an evolutionarily ancient component of innate immunity, is capable of protecting hosts from invading pathogens, either directly, by lysis of target cells, or indirectly, by mobilization of host immune mechanisms. However, this potentially cytotoxic cascade must be tightly regulated, since improperly controlled complement can damage healthy cells and tissues. The practical importance of this axis is highlighted when impairment of complement regulators or bacterial mechanisms of complement evasion result in pathogenic conditions. Recognition of complement as a "double-edged sword" is widely acknowledged, but another, currently underappreciated aspect of complement function has emerged as an important player in homeostatic balance-the dual outcome of complement-mediated inflammation. In most cases, the proinflammatory properties of complement are beneficial to the host. However, certain pathogens have developed the ability to utilize local inflammation as a source of nutrients and as a way to establish a niche for further colonization. Such a strategy can be illustrated in the example of periodontitis. Interestingly, certain tumors also seem to benefit from complement activation products, which promote a proangiogenic and immunosuppressive microenvironment.
MeSH term(s)	Animals ; Biomarkers ; Complement Activation/immunology ; Complement System Proteins/immunology ; Disease Susceptibility/immunology ; Energy Metabolism ; Humans ; Immunity, Innate ; Inflammation/etiology ; Inflammation/metabolism ; Inflammation/pathology ; Neoplasms/etiology ; Neoplasms/metabolism ; Neoplasms/pathology
Chemical Substances	Biomarkers ; Complement System Proteins (9007-36-7)
Language	English
Publishing date	2019-01-10
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2606827-8
ISSN	1664-3224 ; 1664-3224
ISSN (online)	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2018.03125
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Article ; Online: Porphyromonas gingivalis

Prucsi, Zsombor / Zimny, Agnieszka / Płonczyńska, Alicja / Zubrzycka, Natalia / Potempa, Jan / Sochalska, Maja

International journal of molecular sciences

2023 Volume 24, Issue 16

Abstract: Periodontitis is a widespread chronic inflammatory disease caused by a changed dysbiotic oral microbiome. Although multiple species and risk factors are associated with periodontitis, ...

Abstract	Periodontitis is a widespread chronic inflammatory disease caused by a changed dysbiotic oral microbiome. Although multiple species and risk factors are associated with periodontitis,
MeSH term(s)	Humans ; Porphyromonas gingivalis ; Protein-Arginine Deiminases/genetics ; Inflammation ; Periodontitis
Chemical Substances	Protein-Arginine Deiminases (EC 3.5.3.15) ; arginine deiminase (EC 3.5.3.6)
Language	English
Publishing date	2023-08-18
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms241612922
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Article ; Online: Mapping the substrate-binding subsite specificity of a Porphyromonas gingivalis Tpr peptidase.

Staniec, Dominika / Rut, Wioletta / Drag, Marcin / Burmistrz, Michal / Kitching, Michael / Potempa, Jan

Acta biochimica Polonica

2023 Volume 70, Issue 4, Page(s) 963–968

Abstract: Calcium-dependent peptidases of the calpain family are widespread in eukaryotes but uncommon in prokaryotes. A few bacterial calpain homologs have been discovered but none of them have been characterized in detail. Here we present an in-depth substrate ... ...

Abstract	Calcium-dependent peptidases of the calpain family are widespread in eukaryotes but uncommon in prokaryotes. A few bacterial calpain homologs have been discovered but none of them have been characterized in detail. Here we present an in-depth substrate specificity analysis of the bacterial calpain-like peptidase Tpr from Porphyromonas gingivalis. Using the positional scanning hybrid combinatorial substrate library method, we found that the specificity of Tpr peptidase differs substantially from the papain family of cysteine proteases, showing a strong preference for proline residues at positions P2 and P3. Such a degree of specificity indicates that this P. gingivalis cell-surface peptidase has a more sophisticated role than indiscriminate protein degradation to generate peptide nutrients, and may fulfil virulence-related functions such as immune evasion.
MeSH term(s)	Porphyromonas gingivalis/genetics ; Porphyromonas gingivalis/metabolism ; Peptide Hydrolases/metabolism ; Calpain/genetics ; Calpain/metabolism ; Substrate Specificity ; Endopeptidases/metabolism
Chemical Substances	Peptide Hydrolases (EC 3.4.-) ; Calpain (EC 3.4.22.-) ; Endopeptidases (EC 3.4.-)
Language	English
Publishing date	2023-12-08
Publishing country	Poland
Document type	Journal Article
ZDB-ID	595762-x
ISSN	1734-154X ; 0001-527X
ISSN (online)	1734-154X
ISSN	0001-527X
DOI	10.18388/abp.2020_6904
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Zs.B 232: Show issues

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Article ; Online: Gingival fibroblast activation by Porphyromonas gingivalis is driven by TLR2 and is independent of the LPS-TLR4 axis.

Schuster, Aureliusz / Nieboga, Elwira / Kantorowicz, Malgorzata / Lipska, Weronika / Kaczmarzyk, Tomasz / Potempa, Jan / Grabiec, Aleksander M

European journal of immunology

2024 Volume 54, Issue 3, Page(s) e2350776

Abstract: Gingival fibroblasts (GFs) are abundant structural cells of the periodontium that contribute to the host's innate immunity by producing cytokines and chemokines in response to oral pathogens, such as Porphyromonas gingivalis. Isolated lipopolysaccharide ( ...

Abstract	Gingival fibroblasts (GFs) are abundant structural cells of the periodontium that contribute to the host's innate immunity by producing cytokines and chemokines in response to oral pathogens, such as Porphyromonas gingivalis. Isolated lipopolysaccharide (Pg-LPS) is commonly used to study GF responses to P. gingivalis; however, this approach produced conflicting observations regarding its proinflammatory potential and the engagement of specific Toll-like receptors (TLRs). In this work, we demonstrate that commercially available Pg-LPS preparations are weak activators of GF innate immune responses compared with live P. gingivalis or other relevant virulence factors, such as P. gingivalis fimbriae or LPS from Escherichia coli. GF's nonresponsiveness to Pg-LPS can be only partly attributed to the low expression of TLR4 and its accessory molecules, CD14 and LY36, and is likely caused by the unique structure and composition of the Pg-LPS lipid A. Finally, we combined gene silencing and neutralizing antibody studies to demonstrate that GF response to infection with live P. gingivalis relies predominantly on TLR2. In contrast, the LPS-TLR4 signaling plays a negligible role in inflammatory cytokine production by GFs exposed to this oral pathogen, confirming that Pg-LPS stimulation is not an optimal model for studies of GF responses to P. gingivalis.
MeSH term(s)	Lipopolysaccharides ; Porphyromonas gingivalis ; Toll-Like Receptor 2/genetics ; Toll-Like Receptor 2/metabolism ; Toll-Like Receptor 4/metabolism ; Fibroblasts
Chemical Substances	Lipopolysaccharides ; Toll-Like Receptor 2 ; Toll-Like Receptor 4
Language	English
Publishing date	2024-01-08
Publishing country	Germany
Document type	Journal Article
ZDB-ID	120108-6
ISSN	1521-4141 ; 0014-2980
ISSN (online)	1521-4141
ISSN	0014-2980
DOI	10.1002/eji.202350776
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