{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T10:56:49Z","timestamp":1791197809631,"version":"4.1.0"},"reference-count":59,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2004,2,24]],"date-time":"2004-02-24T00:00:00Z","timestamp":1077580800000},"content-version":"vor","delay-in-days":1090,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2001,3]]},"abstract":"<jats:p>\n                    Adherence of pathogenic microorganisms to the cell surface is a key event during infection. We have previously reported the characterization of\n                    <jats:italic>Listeria monocytogenes<\/jats:italic>\n                    transposon mutants defective in adhesion to eukaryotic cells. One of these mutants had lost the ability to produce Ami, a 102\u2003kDa autolytic amidase with an N\u2010terminal catalytic domain and a C\u2010terminal cell wall\u2010anchoring domain made up of repeated modules containing the dipeptide GW (\u2018GW modules\u2019). We generated\n                    <jats:italic>ami<\/jats:italic>\n                    null mutations by plasmid insertion into\n                    <jats:italic>L. monocytogenes<\/jats:italic>\n                    strains lacking the invasion proteins InlA (EGD\u0394\n                    <jats:italic>inlA<\/jats:italic>\n                    ), InlB (EGD\u0394\n                    <jats:italic>inlB<\/jats:italic>\n                    ) or both (EGD\u0394\n                    <jats:italic>inlAB<\/jats:italic>\n                    ). These mutants were 5\u201310 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\u2010anchoring domain fused to the Ami signal peptide. The cell\u2010binding activity of the Ami cell wall\u2010anchoring domain was further demonstrated using the purified polypeptide. Growth of the\n                    <jats:italic>ami<\/jats:italic>\n                    null mutants constructed in EGD and EGD\u0394\n                    <jats:italic>inlAB<\/jats:italic>\n                    backgrounds was attenuated in the livers of mice inoculated intravenously, indicating a role for Ami in\n                    <jats:italic>L. monocytogenes<\/jats:italic>\n                    virulence. Adhesive properties have recently been reported in the non\u2010catalytic domain of two other autolysins,\n                    <jats:italic>Staphylococcus epidermidis<\/jats:italic>\n                    AtlE and\n                    <jats:italic>Staphylococcus saprophyticus<\/jats:italic>\n                    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\u2010positive bacteria.\n                  <\/jats:p>","DOI":"10.1111\/j.1365-2958.2001.02208.x","type":"journal-article","created":{"date-parts":[[2004,12,27]],"date-time":"2004-12-27T16:54:53Z","timestamp":1104166493000},"page":"1212-1224","source":"Crossref","is-referenced-by-count":170,"title":["The autolysin Ami contributes to the adhesion of\n                    <i>Listeria monocytogenes<\/i>\n                    to eukaryotic cells via its cell wall 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