Cited by 251Listeria monocytogenes in Food SafetyBacterial Genetics and BiotechnologyBiochemical and Structural Characterization

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Interaction between the protein InlB of Listeria monocytogenes and lipoteichoic acid: a novel mechanism of protein association at the surface of Gram‐positive bacteria

Jonquières, Renaud, Bierne, Hélène, Fiedler, Franz, Gounon, Pierre, Cossart, Pascale·1999·Molecular Microbiology

DOI 10.1046/j.1365-2958.1999.01652.x

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Abstract

InlB is a Listeria monocytogenes protein that is sufficient to promote entry in a variety of mammalian cells. The last 232‐amino‐acid domain (Csa) of InlB has been shown to mediate attachment on the listerial surface, although its sequence does not suggest any known mechanism of association to the bacterial surface. InlB is present both on the bacterial surface and in culture supernatants. As has been recently demonstrated, both forms of InlB, soluble and surface‐bound, can trigger signalling in host cells. To elucidate the specific role of each of the two forms, it was important to understand how InlB associates with the bacterial surface. Using microscopy, we find evidence that InlB is partially buried in the cell wall layer, and using fractionation experiments we demonstrate that InlB associates with the bacterial cytoplasmic membrane. Moreover, using purified lipoteichoic acid (LTA) and the three polypeptides InlB, Csa, or InlBΔCsa (InlB lacking the last 232 amino acids), we demonstrate that LTA is a ligand for the Csa domain of InlB. These results provide the first evidence of an interaction between lipoteichoic acids and a bacterial protein involved in adhesion and signalling, and highlight a new mechanism of protein association on the surface of Gram‐positive bacteria.

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Authors: Jonquières, R., Bierne, H., Fiedler, F., Gounon, P., & Cossart, P.
Affiliations: Institut Pasteur (FR)
Ludwig-Maximilians-Universität München (DE)
Corresponding author: Cossart, Pascale
ORCID: Bierne, Hélène
Cossart, Pascale
Venue: Molecular Microbiology
Publisher: Wiley
Published: 1999-12
Volume: 34
Issue: 5
Pages: 902-914
ISSN: 0950-382X (ISSN-L)
1365-2958
DOI: 10.1046/j.1365-2958.1999.01652.x
OpenAlex: W1981604960
Cited by: 251
References: 57
Citations by year: 2026: 3 · 2025: 1 · 2024: 2 · 2023: 5 · 2022: 5 · 2021: 4 · 2020: 7 · 2019: 6 · 2018: 7 · 2017: 2 · 2016: 6 · 2015: 7 · 2014: 16 · 2013: 7 · 2012: 10
FWCI: 12.68
Type: journal article
Language: en
Open access: closed
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor, 821 d)
Locations: Molecular Microbiology (publishedVersion)
PubMed (publishedVersion)
Funders: European Commission
Institut National de la Recherche Agronomique
Topics: Life Sciences › Agricultural and Biological Sciences › Food Science › Listeria monocytogenes in Food Safety
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
Keywords: InlB, Listeria monocytogenes, lipoteichoic acid, plasma membrane, bacterial adhesion, host cell signalling, Gram-positive bacteria
MeSH terms: Bacterial Proteins, Cell Fractionation, Cell Membrane, Cell Wall, Chromatography, Gel, Enzyme-Linked Immunosorbent Assay, Fluorescent Antibody Technique, Lipopolysaccharides, Listeria monocytogenes, Membrane Proteins, Plasmids, Protoplasts, Teichoic Acids, Immunoblotting

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Interaction between the protein InlB of Listeria monocytogenes and lipoteichoic acid: a novel mechanism of protein association at the surface of Gram‐positive bacteria

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