ArticleBiological chemistry2010
A novel matrix metalloprotease-like enzyme (karilysin) of the periodontal pathogen Tannerella forsythia ATCC 43037.
Article in Biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 70 citations in OpenAlex.
- Periodontopathogens degrade angiotensin I from the human renin-angiotensin system through surface-attached proteases.Scientific reports · 2025Article
- Microbial Coaggregation in the Oral Cavity: Molecular Interactions and Current Insights.International journal of molecular sciences · 2025Review
- Periodontal Pathogens and Their Links to Neuroinflammation and Neurodegeneration.Microorganisms · 2023Review
- A unique network of attack, defence and competence on the outer membrane of the periodontitis pathogenChemical science · 2023Article
- The Association betweenInternational journal of environmental research and public health · 2022Article
- Latency, thermal stability, and identification of an inhibitory compound of mirolysin, a secretory protease of the human periodontopathogenJournal of enzyme inhibition and medicinal chemistry · 2021Article
- Periodontal Pathogens' strategies disarm neutrophils to promote dysregulated inflammation.Molecular oral microbiology · 2021Review
- Analysis of oral microbiome from fossil human remains revealed the significant differences in virulence factors of modern and ancient Tannerella forsythia.BMC genomics · 2020Article
- Persistence ofCurrent oral health reports · 2020Article
- Article
- An IgY-based immunoassay to evaluate the biomarker potential of the Tannerella forsythia virulence factor karilysin in human saliva.Journal of immunological methods · 2019Article
- The contribution of Tannerella forsythia dipeptidyl aminopeptidase IV in the breakdown of collagen.Molecular oral microbiology · 2018Article
- In vivo expression of proteases and protease inhibitor, a serpin, by periodontal pathogens at teeth and implants.Molecular oral microbiology · 2018Article
- Mirolysin, a LysargiNase from Tannerella forsythia, proteolytically inactivates the human cathelicidin, LL-37.Biological chemistry · 2017Article
- The Type IX Secretion System (T9SS): Highlights and Recent Insights into Its Structure and Function.Frontiers in cellular and infection microbiology · 2017Review
- Outer membrane vesicles of Tannerella forsythia: biogenesis, composition, and virulence.Molecular oral microbiology · 2015Article
- Mirolase, a novel subtilisin-like serine protease from the periodontopathogen Tannerella forsythia.Biological chemistry · 2015Article
- A novel mechanism of latency in matrix metalloproteinases.The Journal of biological chemistry · 2015Article
- KLIKK proteases of Tannerella forsythia: putative virulence factors with a unique domain structure.Frontiers in microbiology · 2015Article
- A pathogenic trace of Tannerella forsythia - shedding of soluble fully active tumor necrosis factor α from the macrophage surface by karilysin.Molecular oral microbiology · 2014Article
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Authors and funding
10 authors at 3 institutions in 3 countries.
Funding
Abstract
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) processed itself into the mature 18-kDa enzyme through sequential autoproteolytic cleavage at both N- and C-terminal profragments. The first cleavage at the Asn14-Tyr15 peptide bond generated the fully active enzyme (47.9 kDa) and subsequent truncations at the C-terminus did not affect proteolytic activity. Mutation of Tyr15 to Ala generated a prokarilysin variant that processed itself into the final 18-kDa form with greatly reduced kinetics. Inactive prokarilysin with the mutated catalytic Glu residue (E136A) was processed by active karilysin at the same sites as the active enzymes. Karilysin proteolytic activity and autoprocessing were inhibited by 1,10-phenanthroline and EDTA. Calcium ions were found to be important for both the activity and thermal stability of karilysin. Using CLiPS technology, the specificity of karilysin was found to be similar to that of MMPs with preference for Leu/Tyr/Met at P1' and Pro/Ala at P3. This specificity and the ability to degrade elastin, fibrinogen and fibronectin may contribute to the pathogenicity of periodontitis.
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