Use of an affinity proteomics approach for the identification of low-abundant bacterial adhesins as applied on the Lewisb-binding adhesin of Helicobacter pylori

Thomas Larsson, Jörgen Bergström, Carol Nilsson, Karl Anders Karlsson

Research output: Contribution to journalArticle

34 Scopus citations

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 Lewisb-binding adhesin of Helicobacter pylori. Protein identification was obtained through the enrichment of approximately 300 fmol of adhesin from solubilized cells. Copyright (C) 2000 Federation of European Biochemical Societies.

Original languageEnglish (US)
Pages (from-to)155-158
Number of pages4
JournalFEBS Letters
Volume469
Issue number2-3
DOIs
StatePublished - Mar 10 2000

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Keywords

  • Bacterial adhesin
  • Helicobacter pylori
  • Low-abundance protein
  • Protein-carbohydrate interaction
  • Proteomics

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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