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Identification of a new sialic acid-binding protein in Helicobacter pylori
Ist Teil von
FEMS immunology and medical microbiology, 2005-05, Vol.44 (2), p.163-169
Ort / Verlag
Oxford, UK: Elsevier B.V
Erscheinungsjahr
2005
Quelle
Oxford Journals 2020 Medicine
Beschreibungen/Notizen
A novel sialic acid-specific lectin has been isolated from
Helicobacter pylori lysate using fetuin–agarose affinity chromatography followed by cleavage of the α(2,3) and α(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.