FEMS immunology and medical microbiology, 2005-05, Vol.44 (2), p.163-169
2005
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Details
- Autor(en) / Beteiligte
- Titel
- 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.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0928-8244eISSN: 1574-695X, 2049-632XDOI: 10.1016/j.femsim.2004.11.008Titel-ID: cdi_proquest_miscellaneous_17848414
- Format
- –
- Schlagworte
- Acids, Affinity chromatography, alpha-Fetoproteins - metabolism, Bacterial Proteins - chemistry, Bacterial Proteins - genetics, Bacterial Proteins - isolation & purification, Bacterial Proteins - metabolism, Cell Line, Tumor, Electrophoresis, Electrophoresis, Polyacrylamide Gel, Exo-a-sialidase, Fetuin-binding, Gel electrophoresis, Glycosphingolipids, Helicobacter pylori, Helicobacter pylori - genetics, Helicobacter pylori - metabolism, Humans, Ionization, Ions, Mass spectrometry, Mass spectroscopy, Molecular weight, Mutagenesis, Site-Directed, Polyacrylamide, Protein adhesin, Protein Binding, Proteins, Recombinant Proteins - metabolism, Sequence Analysis, DNA, Sialic acid-binding, Sialic acid-binding protein, Sialic acids, Sialic Acids - metabolism, Sodium dodecyl sulfate, Sodium lauryl sulfate, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization