ArticleBiological chemistry2017
Mirolysin, a LysargiNase from Tannerella forsythia, proteolytically inactivates the human cathelicidin, LL-37.
Article in Biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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Who cites it
21 citing papers in PubMed, 28 citations in OpenAlex.
- The immune-microbe-metal triad: a vicious cycle driving biomaterial corrosion in the oral inflammatory microenvironment.Bioactive materials · 2027Review
- Fibrinogen was associated with subgingival microbiome in periodontal diseases: a pilot study.Journal of oral microbiology · 2026Article
- Periodontopathogens degrade angiotensin I from the human renin-angiotensin system through surface-attached proteases.Scientific reports · 2025Article
- Expression level and clinical significance of NEAT1 in patients with chronic periodontitis.Journal of dental sciences · 2025Article
- The Proteinase PAPP-A has Deep Evolutionary Roots Outside of the IGF System.Genome biology and evolution · 2025Article
- Leptospira Leptolysin Contributes to Serum Resistance but Is Not Essential for Acute Infection.Molecular microbiology · 2024Article
- The intriguing strategies ofFrontiers in oral health · 2024Article
- A unique network of attack, defence and competence on the outer membrane of the periodontitis pathogenChemical science · 2023Article
- Peptide Stability Is Important but Not a General Requirement for Antimicrobial and Antibiofilm Activity In Vitro and In Vivo.Molecular pharmaceutics · 2023Article
- Shut-Down of Type IX Protein Secretion Alters the Host Immune Response toFrontiers in cellular and infection microbiology · 2022Article
- Leptolysin, aFrontiers in cellular and infection microbiology · 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
- Interactions Between Neutrophils and Periodontal Pathogens in Late-Onset Periodontitis.Frontiers in cellular and infection microbiology · 2021Review
- Tryp-N: A Thermostable Protease for the Production of N-terminal Argininyl and Lysinyl Peptides.Journal of proteome research · 2020Article
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- In vivo expression of proteases and protease inhibitor, a serpin, by periodontal pathogens at teeth and implants.Molecular oral microbiology · 2018Article
- D-Cateslytin, a new antimicrobial peptide with therapeutic potential.Scientific reports · 2017Article
- The Type IX Secretion System (T9SS): Highlights and Recent Insights into Its Structure and Function.Frontiers in cellular and infection microbiology · 2017Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
Abstract
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 activity. The latter metalloprotease, however, was not characterized at the protein level. Therefore, we purified recombinant mirolysin and subjected it to detailed biochemical characterization. Mirolysin was obtained as a 66 kDa zymogen, which autoproteolytically processed itself into a 31 kDa active form via truncations at both the N- and C-termini. Further autodegradation was prevented by calcium. Substrate specificity was determined by the S1' subsite of the substrate-binding pocket, which shows strong preference for Arg and Lys at the carbonyl side of a scissile peptide bond (P1' residue). The protease cleaved an array of host proteins, including human fibronectin, fibrinogen, complement proteins C3, C4, and C5, and the antimicrobial peptide, LL-37. Degradation of LL-37 abolished not only the bactericidal activity of the peptide, but also its ability to bind lipopolysaccharide (LPS), thus quenching the endotoxin proinflammatory activity. Taken together, these results indicate that, through cleavage of LL-37 and complement proteins, mirolysin might be involved in evasion of the host immune response.
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.