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Clostridium difficile secreted Pro-Pro endopeptidase PPEP-1 (ZMP1/CD2830) modulates adhesion through cleavage of the collagen binding protein CD2831
Ist Teil von
FEBS letters, 2015-12, Vol.589 (24), p.3952-3958
Ort / Verlag
England: Elsevier B.V
Erscheinungsjahr
2015
Quelle
MEDLINE
Beschreibungen/Notizen
•C. difficile Pro-Pro endopeptidase (PPEP-1) has a strict preference for cleaving between two prolines.•PPEP-1 has a preference for an Asn at the P2, and a Val, Ile or Leu at the P3 position.•PPEP-1 knockout cells retain the collagen binding protein CD2831 on the cell surface.•PPEP-1 knockout cells show higher affinity for collagen type I.•PPEP-1 knockout cells show attenuated virulence in a hamster infection model.
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.