ArticleMolecular microbiology2011
The structure of the catalytic domain of Tannerella forsythia karilysin reveals it is a bacterial xenologue of animal matrix metalloproteinases.
Article in Molecular microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 28 citations in OpenAlex.
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- A unique network of attack, defence and competence on the outer membrane of the periodontitis pathogenChemical science · 2023Article
- Zymogenic latency in an ∼250-million-year-old astacin metallopeptidase.Acta crystallographica. Section D, Structural biology · 2022Article
- Article
- A structure-derived snap-trap mechanism of a multispecific serpin from the dysbiotic human oral microbiome.The Journal of biological chemistry · 2017Article
- Myroilysin Is a New Bacterial Member of the M12A Family of Metzincin Metallopeptidases and Is Activated by a Cysteine Switch Mechanism.The Journal of 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
- Structural Basis for Latency and Function of Immune Inhibitor A Metallopeptidase, a Modulator of the Bacillus anthracis Secretome.Structure (London, England : 1993) · 2016Article
- Linkages between oral commensal bacteria and atherosclerotic plaques in coronary artery disease patients.NPJ biofilms and microbiomes · 2016Article
- 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
- 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.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
- Functional characterization of Anopheles matrix metalloprotease 1 reveals its agonistic role during sporogonic development of malaria parasites.Infection and immunity · 2014Article
- Architecture and function of metallopeptidase catalytic domains.Protein science : a publication of the Protein Society · 2014Review
- Bioinformatics analysis of bacterial annexins--putative ancestral relatives of eukaryotic annexins.PloS one · 2014Article
- Gingipain-dependent degradation of mammalian target of rapamycin pathway proteins by the periodontal pathogen Porphyromonas gingivalis during invasion.Molecular oral microbiology · 2013Article
- Structure of the catalytic domain of the Tannerella forsythia matrix metallopeptidase karilysin in complex with a tetrapeptidic inhibitor.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- CLCAs - a family of metalloproteases of intriguing phylogenetic distribution and with cases of substituted catalytic sites.PloS one · 2013Article
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Authors and funding
8 authors at 5 institutions in 5 countries.
Funding
Abstract
Metallopeptidases (MPs) are among virulence factors secreted by pathogenic bacteria at the site of infection. One such pathogen is Tannerella forsythia, a member of the microbial consortium that causes peridontitis, arguably the most prevalent infective chronic inflammatory disease known to mankind. The only reported MP secreted by T. forsythia is karilysin, a 52 kDa multidomain protein comprising a central 18 kDa catalytic domain (CD), termed Kly18, flanked by domains unrelated to any known protein. We analysed the 3D structure of Kly18 in the absence and presence of Mg(2+) or Ca(2+) , which are required for function and stability, and found that it evidences most of the structural features characteristic of the CDs of mammalian matrix metalloproteinases (MMPs). Unexpectedly, a peptide was bound to the active-site cleft of Kly18 mimicking a left-behind cleavage product, which revealed that the specificity pocket accommodates bulky hydrophobic side-chains of substrates as in mammalian MMPs. In addition, Kly18 displayed a unique Mg(2+) or Ca(2+) binding site and two flexible segments that could play a role in substrate binding. Phylogenetic and sequence similarity studies revealed that Kly18 is evolutionarily much closer to winged-insect and mammalian MMPs than to potential bacterial counterparts found by genomic sequencing projects. Therefore, we conclude that this first structurally characterized non-mammalian MMP is a xenologue co-opted through horizontal gene transfer during the intimate coexistence between T. forsythia and humans or other animals, in a very rare case of gene shuffling from eukaryotes to prokaryotes. Subsequently, this protein would have evolved in a bacterial environment to give rise to full-length karilysin that is furnished with unique flanking domains that do not conform to the general multidomain architecture of animal MMPs.
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