forsythia/protease

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Identification and characterization of a chymotrypsin-like serine protease from periodontal pathogen, Tannerella forsythia.

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Tannerella forsythia is a bacteria associated with severe periodontal disease. This study reports identification and characterization of a membrane-associated serine protease from T. forsythia. The protease was isolated from T. forsythia membrane fractions and shown to cleave both gelatin and type I

KLIKK proteases of Tannerella forsythia: putative virulence factors with a unique domain structure.

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Comparative genomics of virulent Tannerella forsythia ATCC 43037 and a close health-associated relative, Tannerella BU063, revealed, in the latter, the absence of an entire array of genes encoding putative secretory proteases that possess a nearly identical C-terminal domain (CTD) that ends with a

Mirolase, a novel subtilisin-like serine protease from the periodontopathogen Tannerella forsythia.

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The genome of Tannerella forsythia, an etiological factor of chronic periodontitis, contains several genes encoding putative proteases. Here, we characterized a subtilisin-like serine protease of T. forsythia referred to as mirolase. Recombinant full-length latent promirolase [85 kDa, without its

Miropin, a novel bacterial serpin from the periodontopathogen Tannerella forsythia, inhibits a broad range of proteases by using different peptide bonds within the reactive center loop.

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All prokaryotic genes encoding putative serpins identified to date are found in environmental and commensal microorganisms, and only very few prokaryotic serpins have been investigated from a mechanistic standpoint. Herein, we characterized a novel serpin (miropin) from the human pathogen Tannerella

Prediction of a caspase-like fold in Tannerella forsythia virulence factor PrtH.

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Tannerella forsythia is a bacterial pathogen involved in periodontal disease. A cysteine protease PrtH has been characterized in this bacterium as a virulence factor. PrtH has the activity of detaching adherent cells from substratum, and the level of PrtH is associated with periodontal attachment

The contribution of Tannerella forsythia dipeptidyl aminopeptidase IV in the breakdown of collagen.

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In this study, we characterized a serine protease from Tannerella forsythia that degrades gelatin, type I, and III collagen. Tannerella forsythia is associated with periodontitis progression and severity. The primary goal of this research was to understand the mechanisms by which T. forsythia

Gingipain-dependent augmentation by Porphyromonas gingivalis of phagocytosis of Tannerella forsythia.

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In the pathogenesis of periodontitis, Porphyromonas gingivalis plays a role as a keystone pathogen that manipulates host immune responses leading to dysbiotic oral microbial communities. Arg-gingipains (RgpA and RgpB) and Lys-gingipain (Kgp) are responsible for the majority of bacterial proteolytic

A 5-year longitudinal study of Tannerella forsythia prtH genotype: association with loss of attachment.

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BACKGROUND Tannerella forsythia (previously T. forsythensis) in subgingival plaque has been recognized as a defined periodontal pathogen, but its mere presence may be insufficient for disease initiation and/or progression. The organism may produce a cysteine protease, encoded by the prtH gene, which

Detection of Tannerella forsythia bspA and prtH genotypes among periodontitis patients and healthy subjects-A case-Control study.

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BACKGROUND T. forsythia a gram negative, anaerobe inhabits the mature biofilm present at sites expressing progressive periodontitis. It is a part of "red complex" group which contributes to the pathogenesis of periodontitis. The BspA protein and prtH gene encoded cysteine protease play a vital role

A pathogenic trace of Tannerella forsythia - shedding of soluble fully active tumor necrosis factor α from the macrophage surface by karilysin.

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Tannerella forsythia is implicated as a pathogen causing chronic and aggressive periodontitis. However, its virulence factors, including numerous putative proteases, are mostly uncharacterized. Karilysin is a newly described matrix metalloprotease-like enzyme of T. forsythia. Since pathogen-derived

Proteolytic inactivation of LL-37 by karilysin, a novel virulence mechanism of Tannerella forsythia.

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Tannerella forsythia is a gram-negative bacterium strongly associated with the development and/or progression of periodontal disease. Here, we have shown that a newly characterized matrix metalloprotease-like enzyme, referred to as karilysin, efficiently cleaved the antimicrobial peptide LL-37,

A novel matrix metalloprotease-like enzyme (karilysin) of the periodontal pathogen Tannerella forsythia ATCC 43037.

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Proteases of Tannerella forsythia, a pathogen associated with periodontal disease, are implicated as virulence factors. Here, we characterized a matrix metalloprotease (MMP)-like enzyme of T. forsythia referred to as karilysin. Full-length (without a signal peptide) recombinant karilysin (49.9 kDa)

Mirolysin, a LysargiNase from Tannerella forsythia, proteolytically inactivates the human cathelicidin, LL-37.

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Tannerella forsythia is a periodontal pathogen expressing six secretory proteolytic enzymes with a unique multidomain structure referred to as KLIKK proteases. Two of these proteases, karilysin and mirolysin, were previously shown to protect the bacterium against complement-mediated bactericidal

Analysis of oral microbiome from fossil human remains revealed the significant differences in virulence factors of modern and ancient Tannerella forsythia

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Background: Recent advances in the next-generation sequencing (NGS) allowed the metagenomic analyses of DNA from many different environments and sources, including thousands of years old skeletal remains. It has been shown that most of

Adhesion of Porphyromonas gingivalis and Tannerella forsythia to dentin and titanium with sandblasted and acid etched surface coated with serum and serum proteins - An in vitro study.

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OBJECTIVE To evaluate the adhesion of selected bacterial strains incl. expression of important virulence factors at dentin and titanium SLA surfaces coated with layers of serum proteins. METHODS Dentin- and moderately rough SLA titanium-discs were coated overnight with human serum, or IgG, or human

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