Cited by 185Listeria monocytogenes in Food SafetyBacterial Genetics and BiotechnologyBiochemical and Structural Characterization

The DOI matches its Crossref record; 63 of the 63 references it cites were found in a registry or an index.

The autolysin Ami contributes to the adhesion of Listeria monocytogenes to eukaryotic cells via its cell wall anchor

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Abstract

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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Crossref · 10.1111/j.1365-2958.2001.02208.x

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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].”

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  1. Ward J.B., 1984, Microbial Cell Wall Synthesis and Autolysis., 159

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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
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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