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Updated: Aug 18, 2026

Expression, Purification, and Antimicrobial Activity of S100A12
Published on: May 13, 2017
Identification of a new sialic acid-binding protein in Helicobacter pylori
Hayley J Bennett1, Ian S Roberts
1Faculty of Life Sciences, University of Manchester, 1.800 Stopford Building, Oxford Road, Manchester M13 9PT, UK.
Abstract:
A novel sialic acid-specific lectin has been isolated from Helicobacter pylori lysate using fetuin-agarose affinity chromatography followed by cleavage of the alpha(2,3) and alpha(2,6) linkages of sialic acids using neuraminidase. The protein had a molecular weight of 17.5 kDa on sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE) and was identified by matrix-assisted laser desorption/ionization-time of flight (MALDI-TOF) mass spectrometry to be protein of unknown function with gene number HP0721. Recombinant HP0721 was shown to bind to fetuin-agarose and sialic acid-containing glycosphingolipids on thin-layer plates suggesting this protein may represent another sialic acid-specific adhesin of H. pylori. A H. pylori mutant defective for HP0721 was generated and its ability to bind to human AGS cells assayed.
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