Identification of a new sialic acid-binding protein in Helicobacter pylori.
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.
Bennett
Hayley J
HJ
Faculty of Life Sciences, University of Manchester, 1.800 Stopford Building, Oxford Road, Manchester M13 9PT, UK.
Roberts
Ian S
IS
D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D045744:Cell Line, Tumor; D004591:Electrophoresis, Polyacrylamide Gel; D016480:Helicobacter pylori / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D016297:Mutagenesis, Site-Directed; D011485:Protein Binding; D011994:Recombinant Proteins / Q000378:metabolism; D017422:Sequence Analysis, DNA; D012794:Sialic Acids / Q000378:metabolism*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D000509:alpha-Fetoproteins / Q000378:metabolism
D001426:Bacterial Proteins; D011994:Recombinant Proteins; D012794:Sialic Acids; D000509:alpha-Fetoproteins