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Avall-Jaaskelainen, S., Lindholm, A. and Palva, A. (2003) Surface display of the receptor-binding region of the Lactobacillus brevis S-Layer protein in Lactococcus lactis provides nonadhesive Lactococci with the ability to adhere to intestinal epithelial cells. Applied and Environmental Microbiology, 69, 2230-2236. doi:10.1128/AEM.69.4.2230-2236.2003

has been cited by the following article:

• TITLE: Extraction, purification and identification of surface adhesion ligand from Lactobacillus

  AUTHORS: Xue-Yan Lin, Zhong-Hua Wang, Zhong-Xiang Niu, Jun Peng

  KEYWORDS: Lactobacillus; Adhesion Ligand; Purify; Molecular Weight

  JOURNAL NAME: Advances in Bioscience and Biotechnology, Vol.3 No.3, June 21, 2012

  ABSTRACT: The objective of this experiment was to purify and analyze adhesion protein from the surface of Lactobacillus. The surface adhesion ligand of Lactobacillus was isolated with of LiCl method and (NH4)2SO4 method, followed by sephadex chromatography, analyzed with discontinuous native polyacrylamide gel electrophoresis, and tested with a binding assay with intestinal epithelial cells. We get the adhesion matter by two methods: ammonium sulfate and LiCl extraction. Further purification with sephadex chromatography produced 3 components. The second component of eluted from chromatography had adhesion enhancing ability compared with the control. A single band was present in discontinuous native—poly-acrylamide gel electrophoresis analysis and molecular weight was determined to be 43-66 KDa. The purified adhesion ligand can improve the number of Lactobacillus adhering to the intestinal epithelial cells.