Editor: Wolfgang Kneifel
Binding characteristics of the Lactobacillus brevis ATCC 8287 surface layer to extracellular matrix proteins
Article first published online: 5 JUN 2006
FEMS Microbiology Letters
Volume 260, Issue 2, pages 210–215, July 2006
How to Cite
Leeuw, E. d., Li, X. and Lu, W. (2006), Binding characteristics of the Lactobacillus brevis ATCC 8287 surface layer to extracellular matrix proteins. FEMS Microbiology Letters, 260: 210–215. doi: 10.1111/j.1574-6968.2006.00313.x
- Issue published online: 5 JUN 2006
- Article first published online: 5 JUN 2006
- Received 29 September 2005; revised 5 May 2006; accepted 8 May 2006.First published online 5 June 2006.
- surface layer (S-layer);
- extra-cellular matrix (ECM)
Self-assembling proteins that form crystalline surface layers on many microorganisms can be involved in bacterial-host adhesion via specific interactions with components of the extracellular matrix. Here, we describe the interaction of the Lactobacillus brevis ATCC 8287 surface-layer protein SlpA with fibronectin, laminin, fibrinogen and collagen using surface plasmon resonance. SlpA was found to interact with high affinity to fibronectin and laminin, with a respective binding constant of 89.8 and 26.7 nM. The interaction of SlpA with collagen and fibrinogen was found to be of much lower affinity, with respective binding constants of 31.8 and 26.1 μM. The serine protease inhibitor benzamidine greatly reduced the affinity of SlpA for fibronectin, whereas the affinity for laminin remained unaffected. No protease activity of the purified SlpA protein could be detected. These data suggest that L. brevis may interact with host cells directly through high affinity interactions with laminin and fibronectin predominantly, involving distinct regions of the SlpA protein.