4.3 Article

Selection of peptides that bind to the core oligosaccharide of R-form LPS from a phage-displayed heptapeptide library

Journal

FEMS MICROBIOLOGY LETTERS
Volume 205, Issue 2, Pages 349-354

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1111/j.1574-6968.2001.tb10971.x

Keywords

lipopolysaccharide; core oligosaccharide; random peptide; phage display; Salmonella

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To characterize common sites within the core oligosaccharide of the R-form lipopolysaccharide (LPS), we screened peptides from a phage-displayed heptapeptide library by using the most truncated form of R-LPS, Re-LPS (S. Typhimurium SL1165) as a ligand. After three rounds of biopanning/amplification and subsequent screening by phagemid enzyme-linked immunosorbent assay (ELISA), we selected three distinct clones that bind to the ligand LPS. We characterized the binding sites of the three clones by ELISA and thin-layer chromatography immunostaining and found that the three clones bind the two Re-LPSs (SL1165 and S. Minnesota Re595) and Rb-2-LPS. In addition, one of the clones also bound to S-form. LPS (S. Enteritidis). Current data show that those clones bind to common carbohydrate structure(s) expressed in the core oligosaccharides of those LPS samples. (C) 2001 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.

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