title: 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.
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.
authors.affiliation: Institute of Medical Biochemistry, Göteborg University, Box 440, SE-405 30, Göteborg, Sweden.
authors.forename: T
authors.initials: T
authors.lastname: Larsson
authors.forename: J
authors.initials: J
authors.lastname: Bergström
authors.forename: C
authors.initials: C
authors.lastname: Nilsson
authors.forename: K A
authors.initials: KA
authors.lastname: Karlsson
mesh_terms: D018829:Adhesins, Bacterial / Q000737:chemistry / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D006028:Glycosphingolipids / Q000737:chemistry*; D016480:Helicobacter pylori / Q000737:chemistry*; D006801:Humans; D012709:Serum Albumin / Q000737:chemistry; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D019809:Streptavidin / Q000737:chemistry
chemical_list: D018829:Adhesins, Bacterial; D006028:Glycosphingolipids; C024050:Le(b)-active glycolipid; D012709:Serum Albumin; D019809:Streptavidin