期刊
FEBS LETTERS
卷 589, 期 24, 页码 3952-3958出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2015.10.027
关键词
Bacterial virulence; Secreted protease; Collagen binding; Adhesion; Motility
资金
- MRC [G0601176] Funding Source: UKRI
- Medical Research Council [G0601176] Funding Source: Medline
- Medical Research Council [G0601176] Funding Source: researchfish
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. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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