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Updated: Jun 28, 2025

Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
Published on: January 31, 2014
A conserved strategy to attack collagen: The activator domain in bacterial collagenases unwinds triple-helical
Jamil Serwanja1,2, Alexander C Wieland1,2, Astrid Haubenhofer1,2
1Department of Biosciences and Medical Biology, Paris-Lodron University of Salzburg, Salzburg A-5020, Austria.
Abstract:
Bacterial collagenases are important virulence factors, secreted by several pathogenic Clostridium, Bacillus, Spirochaetes, and Vibrio species. Yet, the mechanism by which these enzymes cleave collagen is not well understood. Based on biochemical and mutational studies we reveal that collagenase G (ColG) from Hathewaya histolytica recognizes and processes collagen substrates differently depending on their nature (fibrillar vs. soluble collagen); distinct dynamic interactions between the activator and peptidase domain are required based on the substrate type. Using biochemical and circular dichroism studies, we identify the presumed noncatalytic activator domain as the single-domain triple helicase that unwinds collagen locally, transiently, and reversibly.
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