Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8383992 | FEBS Letters | 2015 | 7 Pages |
Abstract
The Clostridium difficile cd2830 gene product is a secreted metalloprotease, named Pro-Pro endopeptidase (PPEP-1). PPEP-1 cleaves C. difficile cell surface proteins (e.g. CD2831). Here, we confirmed that PPEP-1 has a unique preference for prolines surrounding the scissile bond. Moreover, we show that it exhibits a high preference for an asparagine at the P2 position and hydrophobic residues at the P3 position. Using a PPEP-1 knockout C. difficile strain, we demonstrate that the removal of the collagen binding protein CD2831 is fully attributable to PPEP-1 activity. The PPEP-1 knockout strain demonstrated higher affinity for collagen type I with attenuated virulence in hamsters.
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Authors
Paul J. Hensbergen, Oleg I. Klychnikov, Dennis Bakker, Irina Dragan, Michelle L. Kelly, Nigel P. Minton, Jeroen Corver, Ed J. Kuijper, Jan Wouter Drijfhout, Hans C. van Leeuwen,