Abstract
Bacterial collagenases involved in donor infection are widely applied in many fields due to their high activity and specificity; however, little is known regarding the mechanisms by which bacterial collagenases degrade insoluble collagen in host tissues. Using high-speed atomic force microscopy, we simultaneously visualized the hierarchical structure of collagen fibrils and the movement of a representative bacterial collagenase, Clostridium histolyticum type I collagenase (ColG), to determine the relationship between collagen structure and collagenase movement. Notably, ColG moved ~14.5 nm toward the collagen N terminus in ~3.8 s in a manner dependent on a catalytic zinc ion. While ColG was engaged, collagen molecules were not only degraded but also occasionally rearranged to thicken neighboring collagen fibrils. Importantly, we found a similarity of relationship between the enzyme-substrate interface structure and enzyme migration in collagen-collagenase and DNA-nuclease systems, which share a helical substrate structure, suggesting a common strategy in enzyme evolution.
Highlights
Bacterial collagenases involved in donor infection are widely applied in many fields due to their high activity and specificity; little is known regarding the mechanisms by which bacterial collagenases degrade insoluble collagen in host tissues
Rat tail type I collagen molecules were gradually aligned and assembled into a long, narrow sheet-like structure (Supplementary Fig. 1 and Supplementary Movie 1). The orientation of these assemblies can be controlled by hydrodynamic flow[23], but the orientation was not controlled in our study
These features in the individual fibril were consistent with a minimal collagen fibril assembled from two microfibrils that are each composed of five tropocollagen molecules[22]
Summary
Bacterial collagenases involved in donor infection are widely applied in many fields due to their high activity and specificity; little is known regarding the mechanisms by which bacterial collagenases degrade insoluble collagen in host tissues. The highly studied Clostridium histolyticum collagenases degrade collagen fibrils far more efficiently than vertebrate collagenases, known as matrix metalloproteinases (MMPs)[3]. Due to their specificity and high activity, clostridial collagenases are widely applied in various fields, including enzymatic wound debridement and fibroproliferative disorder therapy in healthcare, meat tenderization in the food industry, unhairing and dye diffusion processes in the leather industry, and the isolation of animal cells and tissues in scientific research[1]. The collagen binding domains (CBDs) of clostridial collagenase are not necessary to process soluble collagen molecules[9], they www.nature.com/scientificreports/
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