Cited by 199Listeria monocytogenes in Food SafetyAdvanced Proteomics Techniques and ApplicationsBacterial Genetics and Biotechnology

The cell wall subproteome of Listeria monocytogenes

Schaumburg, Jessica, Diekmann, Oliver, Hagendorff, Petra, Bergmann, Simone, Rohde, Manfred, Hammerschmidt, Sven, Jänsch, Lothar, Wehland, Jürgen +1 more·2004·PROTEOMICS

Abstract

The surface subproteome of Listeria monocytogenes that includes many proteins already known to be involved in virulence and interaction with host cells has been characterized. A new method for the isolation of a defined surface proteome of low complexity has been established based on serial extraction of proteins by different salts at high concentration, and in all 55 proteins were identified by N-terminal sequencing and mass spectrometry. About 16% of these proteins are of unknown function and three proteins have no orthologue in the nonpathogenic L. innocua and might be involved in virulence mechanisms. Remarkably, a relatively high number of proteins with a function in the cytoplasmic compartment was identified in this surface proteome. These proteins had neither predicted or detectable signal peptides nor could any modification be observed except removal of the N-terminal methionine. Enolase (Lmo2455) is one of these proteins. It was shown to be present in the cell wall of the pathogen by immunoelectron microscopy and, along with heat shock factor DnaK (Lmo1473), elongation factor TU (Lmo2653), and glyceraldehyde-3-phosphate dehydrogenase (Lmo2459), it was found to be able to bind human plasminogen in overlay blots and surface plasmon resonance (SPR) experiments. The KD values of these interactions were determined by SPR measurements. The data indicate a possible role of these proteins as receptors for human plasminogen on the bacterial cell surface. The potential role of this recruitment of a host protease for extracellular invasion mechanisms is discussed.

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Crossref · 10.1002/pmic.200400928

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Authors
Schaumburg, J., Diekmann, O., Hagendorff, P., Bergmann, S., Rohde, M., Hammerschmidt, S., Jänsch, L., Wehland, J., & Kärst, U.
Affiliations
  • Lund University (SE)
  • Biaffin (Germany) (DE)
  • Helmholtz Centre for Infection Research (DE)
Corresponding author
Kärst, Uwe
Venue
PROTEOMICS
Publisher
Wiley
Published
2004-10
Volume
4
Issue
10
Pages
2991-3006
ISSN
  • 1615-9853 (ISSN-L)
  • 1615-9861
OpenAlex
W2003688768
Cited by
199
References
58
Citations by year
2026: 1 · 2025: 3 · 2024: 6 · 2023: 3 · 2022: 1 · 2021: 2 · 2020: 3 · 2019: 9 · 2018: 2 · 2017: 7 · 2016: 6 · 2015: 11 · 2014: 22 · 2013: 15 · 2012: 18
FWCI
10.21
Type
journal article
Language
en
Open access
closed
Locations
  • PROTEOMICS (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Listeria monocytogenes in Food Safety
  • Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Keywords
Listeria monocytogenes, cell surface proteome, virulence factors, plasminogen binding, enolase, DnaK, elongation factor Tu, glyceraldehyde-3-phosphate dehydrogenase, cytosolic proteins, host-pathogen interaction, plasminogen receptor, Listeria innocua
MeSH terms
Aminopeptidases, Bacterial Proteins, Cell Wall, Cloning, Molecular, Cytoplasm, Electrophoresis, Polyacrylamide Gel, Escherichia coli, Humans, Kinetics, Ligands, Listeria monocytogenes, Methionine, Plasminogen, Proteins, Salts, Mass Spectrometry, Time Factors, Virulence, Blotting, Western, Electrophoresis, Gel, Two-Dimensional, Microscopy, Immunoelectron, Protein Structure, Tertiary, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Computational Biology, Surface Plasmon Resonance, Sequence Analysis, Protein, Proteome

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