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Use of an affinity proteomics approach for the identification of low-abundant bacterial adhesins as applied on the Lewis(b)-binding adhesin of Helicobacter pylori.

Journal article
Authors Thomas Larsson
Jörgen Bergström
Carol L Nilsson
Karl-Anders Karlsson
Published in FEBS letters
Volume 469
Issue 2-3
Pages 155-8
ISSN 0014-5793
Publication year 2000
Published at Institute of Medical Biochemistry
Pages 155-8
Language en
Keywords Adhesins, Bacterial, chemistry, isolation & purification, Electrophoresis, Polyacrylamide Gel, Glycosphingolipids, chemistry, Helicobacter pylori, chemistry, Humans, Serum Albumin, chemistry, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Streptavidin, chemistry
Subject categories Chemistry


Microbial attachment to host cell surfaces is considered to be the first essential step for colonization and infection. In most known cases, attachment is mediated by a specific protein-carbohydrate interaction. We have used a carbohydrate-containing crosslinking probe to select bacterial surface adhesins for trypsin digestion, MALDI-TOF mass spectrometry and identification against genome sequence. The present paper describes this functional proteomics approach for identification of the recently cloned low-abundant Lewis(b)-binding adhesin of Helicobacter pylori. Protein identification was obtained through the enrichment of approximately 300 fmol of adhesin from solubilized cells.

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