ArticleFrontiers in microbiology2015
KLIKK proteases of Tannerella forsythia: putative virulence factors with a unique domain structure.
Article in Frontiers in microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 57 citations in OpenAlex.
- Interspecies regulation of virulence through gingipain inhibition by a Tannerella forsythia serpin.EMBO reports · 2026Article
- Ancient Species Diversity and Niche Adaptation in Tannerella and Porphyromonas Revealed Through Pangenomics.Genome biology and evolution · 2026Article
- The impact of organ transplantation on changes in the oral microbiome, particularly on bacteria causing periodontal inflammation - narrative review.Frontiers in cellular and infection microbiology · 2026Review
- Periodontopathogens degrade angiotensin I from the human renin-angiotensin system through surface-attached proteases.Scientific reports · 2025Article
- Microbiological and molecular aspects of periodontitis pathogenesis: an infection-induced inflammatory condition.Frontiers in cellular and infection microbiology · 2025Review
- Nisin, a Probiotic Bacteriocin, Modulates the Inflammatory and Microbiome Changes in Female Reproductive Organs Mediated by Polymicrobial Periodontal Infection.Microorganisms · 2024Article
- Structural and functional insights into the C-terminal signal domain of the Bacteroidetes type-IX secretion system.Open biology · 2024Article
- Ancient Genomes From Bronze Age Remains Reveal Deep Diversity and Recent Adaptive Episodes for Human Oral Pathobionts.Molecular biology and evolution · 2024Article
- Screening and characterization of aptamers recognizing the periodontal pathogen Tannerella forsythia.FEBS open bio · 2024Article
- The intriguing strategies ofFrontiers in oral health · 2024Article
- Investigating the role of aFrontiers in oral health · 2024Article
- Multispecies biofilm behavior and host interaction support the association of Tannerella serpentiformis with periodontal health.Molecular oral microbiology · 2023Article
- A unique network of attack, defence and competence on the outer membrane of the periodontitis pathogenChemical science · 2023Article
- The type IX secretion system: Insights into its function and connection to glycosylation inEngineering microbiology · 2022Review
- Riemerella anatipestifer T9SS Effector SspA Functions in Bacterial Virulence and Defending Natural Host Immunity.Applied and environmental microbiology · 2022Article
- Recent developments in systems biology and genetic engineering toward design of vaccines for TB.Critical reviews in biotechnology · 2022Review
- Shut-Down of Type IX Protein Secretion Alters the Host Immune Response toFrontiers in cellular and infection microbiology · 2022Article
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- 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
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
Abstract
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 -Lys-Leu-Ile-Lys-Lys motif. This observation suggests that these proteins, referred to as KLIKK proteases, may function as virulence factors. Re-sequencing of the loci of the KLIKK proteases found only six genes grouped in two clusters. All six genes were expressed by T. forsythia in routine culture conditions, although at different levels. More importantly, a transcript of each gene was detected in gingival crevicular fluid (GCF) from periodontitis sites infected with T. forsythia indicating that the proteases are expressed in vivo. In each protein, a protease domain was flanked by a unique N-terminal profragment and a C-terminal extension ending with the CTD. Partially purified recombinant proteases showed variable levels of proteolytic activity in zymography gels and toward protein substrates, including collagen, gelatin, elastin, and casein. Taken together, these results indicate that the pathogenic strain of T. forsythia secretes active proteases capable of degrading an array of host proteins, which likely represents an important pathogenic feature of this bacterium.
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