Difference between revisions of "Part:BBa K2328007"

Latest revision as of 09:49, 13 October 2017

LcsB

anchoring protein and structure

Multiple sequence alignment revealed that the C-terminal region (LcsB) of Lb. crispatus K2-4-3 SlpB had a high similarity with the cell wall binding domains SA and CbsA of Lactobacillus acidophilus and Lb. crispatus.

Usage and Biology

To evaluate the potential application as an anchoring protein, the foreign protein was fused to the N-terminus of the LcsB region, and the fused proteins will be successfully produced in Escherichia coli, respectively. After mixing them with the non-genetically modified lactic acid bacteria cells，the protein-LcsB were functionally associated with the cell surface of various lactic acid bacteria tested. In addition, the binding capacity could be improved by SDS pretreatment. Moreover, both of the fused proteins could simultaneously bind to the surface of a single cell.

Reference

[1] Hu S, et al. Heterologous protein display on the cell surface of lactic acid bacteria mediated by the s-layer protein.Microb Cell Fact. 2011.

Sequence and Features