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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
Links www.ncbi.nlm.nih.gov/entrez/query.f...
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

Abstract

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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