Selection of peptides that bind to the core oligosaccharide of R-form LPS from a phage-displayed heptapeptide library.
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 Rb2-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.
Noda
K
K
Department of Biochemistry and Biotechnology, Tottori University, 680-8553, Tottori, Japan.
Yamasaki
R
R
Hironaka
Y
Y
Kitagawa
A
A
D008024:Ligands; D008070:Lipopolysaccharides / Q000378:metabolism*; D009844:Oligosaccharides / Q000378:metabolism*; D019151:Peptide Library; D010455:Peptides / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D011485:Protein Binding
D008024:Ligands; D008070:Lipopolysaccharides; D009844:Oligosaccharides; D019151:Peptide Library; D010455:Peptides