A novel matrix metalloprotease-like enzyme (karilysin) of the periodontal pathogen Tannerella forsythia ATCC 43037
-
Abdulkarim Y. Karim
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.
©2010 by Walter de Gruyter Berlin New York
Articles in the same Issue
- REVIEW
- Hexose-6-phosphate dehydrogenase in the endoplasmic reticulum
- GENES AND NUCLEIC ACIDS
- Biochemical characterization of human Ecdysoneless reveals a role in transcriptional regulation
- PROTEIN STRUCTURE AND FUNCTION
- Bovine β-lactoglobulin acts as an acid-resistant drug carrier by exploiting its diverse binding regions
- Structural studies of the phosphatidylinositol 3-kinase (PI3K) SH3 domain in complex with a peptide ligand: role of the anchor residue in ligand binding
- A fluorescence correlation spectroscopy study of ligand interaction with cytokinin-specific binding protein from mung bean
- The oxygen-independent coproporphyrinogen III oxidase HemN utilizes harderoporphyrinogen as a reaction intermediate during conversion of coproporphyrinogen III to protoporphyrinogen IX
- MEMBRANES, LIPIDS, GLYCOBIOLOGY
- Phytosphingosine kills Candida albicans by disrupting its cell membrane
- CELL BIOLOGY AND SIGNALING
- Dexamethasone-dependent versus -independent markers of epithelial to mesenchymal transition in primary hepatocytes
- PROTEOLYSIS
- Potential role of multiple members of the kallikrein-related peptidase family of serine proteases in activating latent TGFβ1 in semen
- Binding and activation of the human plasma kinin-forming system on the cell walls of Candida albicans and Candida tropicalis
- A novel matrix metalloprotease-like enzyme (karilysin) of the periodontal pathogen Tannerella forsythia ATCC 43037
- NOVEL TECHNIQUES
- CYP21-catalyzed production of the long-term urinary metandienone metabolite 17β-hydroxymethyl-17α-methyl-18-norandrosta-1,4,13-trien-3-one: a contribution to the fight against doping
Articles in the same Issue
- REVIEW
- Hexose-6-phosphate dehydrogenase in the endoplasmic reticulum
- GENES AND NUCLEIC ACIDS
- Biochemical characterization of human Ecdysoneless reveals a role in transcriptional regulation
- PROTEIN STRUCTURE AND FUNCTION
- Bovine β-lactoglobulin acts as an acid-resistant drug carrier by exploiting its diverse binding regions
- Structural studies of the phosphatidylinositol 3-kinase (PI3K) SH3 domain in complex with a peptide ligand: role of the anchor residue in ligand binding
- A fluorescence correlation spectroscopy study of ligand interaction with cytokinin-specific binding protein from mung bean
- The oxygen-independent coproporphyrinogen III oxidase HemN utilizes harderoporphyrinogen as a reaction intermediate during conversion of coproporphyrinogen III to protoporphyrinogen IX
- MEMBRANES, LIPIDS, GLYCOBIOLOGY
- Phytosphingosine kills Candida albicans by disrupting its cell membrane
- CELL BIOLOGY AND SIGNALING
- Dexamethasone-dependent versus -independent markers of epithelial to mesenchymal transition in primary hepatocytes
- PROTEOLYSIS
- Potential role of multiple members of the kallikrein-related peptidase family of serine proteases in activating latent TGFβ1 in semen
- Binding and activation of the human plasma kinin-forming system on the cell walls of Candida albicans and Candida tropicalis
- A novel matrix metalloprotease-like enzyme (karilysin) of the periodontal pathogen Tannerella forsythia ATCC 43037
- NOVEL TECHNIQUES
- CYP21-catalyzed production of the long-term urinary metandienone metabolite 17β-hydroxymethyl-17α-methyl-18-norandrosta-1,4,13-trien-3-one: a contribution to the fight against doping
