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The autolysin Ami contributes to the adhesion of Listeria monocytogenes to eukaryotic cells via its cell wall anchor
Open accessAbstract
Adherence of pathogenic microorganisms to the cell surface is a key event during infection. We have previously reported the characterization of Listeria monocytogenes transposon mutants defective in adhesion to eukaryotic cells. One of these mutants had lost the ability to produce Ami, a 102 kDa autolytic amidase with an N‐terminal catalytic domain and a C‐terminal cell wall‐anchoring domain made up of repeated modules containing the dipeptide GW (‘GW modules’). We generated ami null mutations by plasmid insertion into L. monocytogenes strains lacking the invasion proteins InlA (EGDΔ inlA ), InlB (EGDΔ inlB ) or both (EGDΔ inlAB ). These mutants were 5–10 times less adherent than their parental strains in various cell types. The adhesion capacity of the mutants was restored by complementation with a DNA fragment encoding the Ami cell wall‐anchoring domain fused to the Ami signal peptide. The cell‐binding activity of the Ami cell wall‐anchoring domain was further demonstrated using the purified polypeptide. Growth of the ami null mutants constructed in EGD and EGDΔ inlAB backgrounds was attenuated in the livers of mice inoculated intravenously, indicating a role for Ami in L. monocytogenes virulence. Adhesive properties have recently been reported in the non‐catalytic domain of two other autolysins, Staphylococcus epidermidis AtlE and Staphylococcus saprophyticus Aas. Interestingly, we found that these domains were also composed of repeated GW modules. Thus, certain autolysins appear to promote bacterial attachment by means of their GW repeat domains. These molecules may contribute to the colonization of host tissues by Gram‐positive bacteria.
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Autolysins of Staphylococcus epidermidis affect primary attachment to solid surfaces, and the autolysin of Listeria monocytogenes contributes to adhesion to eucaryotic cells.
“For example, autolysins of Staphylococcus epidermidis were recently shown to affect primary attachment to solid surfaces, and the autolysin of Listeria monocytogenes contributes to adhesion to eucaryotic cells [44,45].”
From Positive role of cell wall anchored proteinase PrtP in adhesion of lactococci (2007) · cites this paper as [45]
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The cell wall subproteome of Listeria monocytogenes
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Positive role of cell wall anchored proteinase PrtP in adhesion of lactococci
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“For example, autolysins of Staphylococcus epidermidis were recently shown to affect primary attachment to solid surfaces, and the autolysin of Listeria monocytogenes contributes to adhesion to eucaryotic cells [44,45].”
Background
Metadata
- Authors
- Milohanic, E., Jonquières, R., Cossart, P., Berche, P., & Gaillard, J.
- Affiliations
- Inserm (FR)
- Institut Pasteur (FR)
- Corresponding author
- Gaillard, Jean‐Louis
- Venue
- Molecular Microbiology
- Publisher
- Wiley
- Published
- 2001-03
- Volume
- 39
- Issue
- 5
- Pages
- 1212-1224
- ISSN
- 0950-382X (ISSN-L)
- 1365-2958
- OpenAlex
- W2128037586
- Cited by
- 185
- References
- 63
- Citations by year
- 2026: 4 · 2025: 3 · 2024: 3 · 2023: 5 · 2022: 2 · 2021: 5 · 2020: 3 · 2019: 6 · 2018: 4 · 2017: 2 · 2016: 5 · 2015: 3 · 2014: 12 · 2013: 6 · 2012: 9
- FWCI
- 10.92
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Molecular Microbiology (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- 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
- Listeria monocytogenes, bacterial adhesion, cell surface binding, integrated nested Laplace approximation, InlB, virulence, complementation
- MeSH terms
- Amino Acid Sequence, Animals, Bacterial Adhesion, Cell Wall, Eukaryotic Cells, Female, Humans, Listeriosis, Listeria monocytogenes, Molecular Sequence Data, Mutation, N-Acetylmuramoyl-L-alanine Amidase, Tumor Cells, Cultured, Virulence, Sequence Alignment, Mice
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