{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T06:23:25Z","timestamp":1790490205932,"version":"4.1.0"},"reference-count":29,"publisher":"Microbiology Society","issue":"6","funder":[{"name":"Minist\u00e8re de l'enseignment sup\u00e9rieur, de la recherche et de l'innovation"},{"name":"Minist\u00e8re de l\u02bcenseignement sup\u00e9rieur, de la recherche et de l\u02bcInnovation"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2020,6,1]]},"abstract":"<jats:p>\n                  <jats:italic>\n                     <jats:named-content content-type=\"species\">\n                        <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"uri\" xlink:href=\"http:\/\/doi.org\/10.1601\/nm.3924\" xlink:type=\"simple\">Clostridium difficile<\/jats:ext-link>\n                     <\/jats:named-content>\n                  <\/jats:italic> 630 possesses a cryptic but functional gene cluster <jats:italic>vanG<\/jats:italic>\n                  <jats:sub>Cd<\/jats:sub> homologous to the <jats:italic>vanG<\/jats:italic> operon of <jats:italic>\n                     <jats:named-content content-type=\"species\">\n                        <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"uri\" xlink:href=\"http:\/\/doi.org\/10.1601\/nm.5526\" xlink:type=\"simple\">Enterococcus faecalis<\/jats:ext-link>\n                     <\/jats:named-content>\n                  <\/jats:italic>. Expression of <jats:italic>vanG<\/jats:italic>\n                  <jats:sub>Cd<\/jats:sub> in the presence of subinhibitory concentrations of vancomycin is accompanied by peptidoglycan amidation on the <jats:italic>meso<\/jats:italic>-DAP residue. In this paper, we report the presence of two potential asparagine synthetase genes named <jats:italic>asnB<\/jats:italic> and <jats:italic>asnB2<\/jats:italic> in the <jats:italic>\n                     <jats:named-content content-type=\"species\">\n                        <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"uri\" xlink:href=\"http:\/\/doi.org\/10.1601\/nm.3924\" xlink:type=\"simple\">C. difficile<\/jats:ext-link>\n                     <\/jats:named-content>\n                  <\/jats:italic> genome whose products were potentially involved in this peptidoglycan structure modification. We found that <jats:italic>asnB<\/jats:italic> expression was only induced when <jats:italic>\n                     <jats:named-content content-type=\"species\">\n                        <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"uri\" xlink:href=\"http:\/\/doi.org\/10.1601\/nm.3924\" xlink:type=\"simple\">C. difficile<\/jats:ext-link>\n                     <\/jats:named-content>\n                  <\/jats:italic> was grown in the presence of vancomycin, yet independently from the <jats:italic>vanG<\/jats:italic>\n                  <jats:sub>Cd<\/jats:sub> resistance and regulation operons. In addition, peptidoglycan precursors were not amidated when <jats:italic>asnB<\/jats:italic> was inactivated. No change in vancomycin MIC was observed in the <jats:italic>asnB<\/jats:italic> mutant strain. In contrast, overexpression of <jats:italic>asnB<\/jats:italic> resulted in the amidation of most of the <jats:italic>\n                     <jats:named-content content-type=\"species\">\n                        <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"uri\" xlink:href=\"http:\/\/doi.org\/10.1601\/nm.3924\" xlink:type=\"simple\">C. difficile<\/jats:ext-link>\n                     <\/jats:named-content>\n                  <\/jats:italic> peptidoglycan precursors and in a weak increase of vancomycin susceptibility. AsnB activity was confirmed in <jats:italic>\n                     <jats:named-content content-type=\"species\">\n                        <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"uri\" xlink:href=\"http:\/\/doi.org\/10.1601\/nm.3093\" xlink:type=\"simple\">E. coli<\/jats:ext-link>\n                     <\/jats:named-content>\n                  <\/jats:italic>. In contrast, the expression of the second asparagine synthetase, AsnB2, was not induced in the presence of vancomycin. In summary, our results demonstrate that AsnB is responsible for peptidoglycan amidation of <jats:italic>\n                     <jats:named-content content-type=\"species\">\n                        <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"uri\" xlink:href=\"http:\/\/doi.org\/10.1601\/nm.3924\" xlink:type=\"simple\">C. difficile<\/jats:ext-link>\n                     <\/jats:named-content>\n                  <\/jats:italic> in the presence of vancomycin.<\/jats:p>","DOI":"10.1099\/mic.0.000917","type":"journal-article","created":{"date-parts":[[2020,5,7]],"date-time":"2020-05-07T07:38:26Z","timestamp":1588837106000},"page":"567-578","source":"Crossref","is-referenced-by-count":12,"title":["AsnB is responsible for peptidoglycan precursor amidation in Clostridium difficile in the presence of vancomycin"],"prefix":"10.1099","volume":"166","author":[{"given":"Fariza","family":"Ammam","sequence":"first","affiliation":[{"name":"Present address: Department of Engineering Science, University of Oxford, Parks Road, Oxford,OX1 3PJ, UK"},{"name":"Universit\u00e9 Paris-Saclay, INRAE, AgroParisTech, Micalis Institute, Jouy en Josas, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Delphine","family":"Patin","sequence":"additional","affiliation":[{"name":"Universit\u00e9 Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), 91198, Gif-sur-Yvette, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4582-0585","authenticated-orcid":false,"given":"H\u00e9loise","family":"Coullon","sequence":"additional","affiliation":[{"name":"Present address: Division of Infectious Diseases, Department of Medicine, Washington University, School of Medicine, St. Louis, MO, USA"},{"name":"Universit\u00e9 Paris-Saclay, INRAE, AgroParisTech, Micalis Institute, Jouy en Josas, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6154-9107","authenticated-orcid":false,"given":"Didier","family":"Blanot","sequence":"additional","affiliation":[{"name":"Universit\u00e9 Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), 91198, Gif-sur-Yvette, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thierry","family":"Lambert","sequence":"additional","affiliation":[{"name":"Universit\u00e9 Paris-Saclay, INRAE, AgroParisTech, Micalis Institute, Jouy en Josas, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3205-0275","authenticated-orcid":false,"given":"Dominique","family":"Mengin-Lecreulx","sequence":"additional","affiliation":[{"name":"Universit\u00e9 Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), 91198, Gif-sur-Yvette, 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