Bacterial enzymes and dentinal matrix proteins

Bacterial enzymes involved in dental caries primarily include collagenolytic proteases (such as M9 family metalloproteases and U32 family enzymes), which are produced by oral bacteria, notably Clostridium histolyticum, Porphyromonas, and Treponema denticola. These enzymes directly degrade dentinal matrix proteins such as type I collagen and members of the SIBLING family, facilitating the spread of bacteria and progression of carious lesions. Alongside bacterial proteases, host-derived matrix metalloproteinases (MMPs) substantially contribute to dentinal matrix breakdown following acid-mediated demineralization, further releasing bioactive matrix components with potential roles in reparative dentinogenesis or modulation of inflammation. Collectively, these proteases and their activity on dentinal matrix proteins constitute key targets for therapeutic strategies in the management of dental caries, targeting either enzyme inhibition or stabilization of matrix components to slow disease progression and promote tissue repair.

Other names

Bacterial collagenolytic proteasesMicrobial collagenasesMatrix metalloproteinases (for host enzymes)Dentin matrix components (DMCs)

Enzyme inhibition (blocking bacterial or host matrix metalloproteinases to prevent matrix breakdown); Metal ion chelation (e.g., zinc chelation to inhibit enzyme activity)