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 Citations (Scopus)

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
Externally publishedYes

Fingerprint

Bacterial Adhesins
Helicobacter pylori
Proteomics
Carbohydrates
Matrix-Assisted Laser Desorption-Ionization Mass Spectrometry
Crosslinking
Trypsin
Mass spectrometry
Digestion
Mass Spectrometry
Proteins
Genes
Genome
Infection
Helicobacter adhesin

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Use of an affinity proteomics approach for the identification of low-abundant bacterial adhesins as applied on the Lewisb-binding adhesin of Helicobacter pylori. / Larsson, Thomas; Bergström, Jörgen; Nilsson, Carol; Karlsson, Karl Anders.

In: FEBS Letters, Vol. 469, No. 2-3, 10.03.2000, p. 155-158.

Research output: Contribution to journalArticle

Larsson, Thomas ; Bergström, Jörgen ; Nilsson, Carol ; Karlsson, Karl Anders. / Use of an affinity proteomics approach for the identification of low-abundant bacterial adhesins as applied on the Lewisb-binding adhesin of Helicobacter pylori. In: FEBS Letters. 2000 ; Vol. 469, No. 2-3. pp. 155-158.
@article{b57ae772105c47f2ae040631ef7ab999,
title = "Use of an affinity proteomics approach for the identification of low-abundant bacterial adhesins as applied on the Lewisb-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 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.",
keywords = "Bacterial adhesin, Helicobacter pylori, Low-abundance protein, Protein-carbohydrate interaction, Proteomics",
author = "Thomas Larsson and J{\"o}rgen Bergstr{\"o}m and Carol Nilsson and Karlsson, {Karl Anders}",
year = "2000",
month = "3",
day = "10",
doi = "10.1016/S0014-5793(00)01270-9",
language = "English (US)",
volume = "469",
pages = "155--158",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "2-3",

}

TY - JOUR

T1 - Use of an affinity proteomics approach for the identification of low-abundant bacterial adhesins as applied on the Lewisb-binding adhesin of Helicobacter pylori

AU - Larsson, Thomas

AU - Bergström, Jörgen

AU - Nilsson, Carol

AU - Karlsson, Karl Anders

PY - 2000/3/10

Y1 - 2000/3/10

N2 - 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.

AB - 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.

KW - Bacterial adhesin

KW - Helicobacter pylori

KW - Low-abundance protein

KW - Protein-carbohydrate interaction

KW - Proteomics

UR - http://www.scopus.com/inward/record.url?scp=0034629005&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034629005&partnerID=8YFLogxK

U2 - 10.1016/S0014-5793(00)01270-9

DO - 10.1016/S0014-5793(00)01270-9

M3 - Article

VL - 469

SP - 155

EP - 158

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 2-3

ER -