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The role of autolysis during gonococcal\ninfection is not known, but possible advantages for the bacterial\npopulation include provision of nutrients to a starving population,\nmodulation of the host immune response by released cell components, and\ndonation of DNA for natural transformation. Biochemical studies\nindicated that an\n                    <jats:italic>N<\/jats:italic>\n                    -acetylmuramyl-\n                    <jats:sc>l<\/jats:sc>\n                    -alanine amidase\nis responsible for cell wall breakdown during autolysis. In order to\nbetter understand autolysis and in hopes of creating a nonautolytic\nmutant, we mutated\n                    <jats:italic>amiC<\/jats:italic>\n                    , the gene for a putative\npeptidoglycan-degrading amidase in\n                    <jats:italic>N. gonorrhoeae<\/jats:italic>\n                    .\nCharacterization of peptidoglycan fragments released during growth\nshowed that an\n                    <jats:italic>amiC<\/jats:italic>\n                    mutant did not produce free disaccharide,\nconsistent with a role for AmiC as an\n                    <jats:italic>N<\/jats:italic>\n                    -acetylmuramyl-\n                    <jats:sc>l<\/jats:sc>\n                    -alanine amidase. Compared to the\nwild-type parent, the mutant exhibited altered growth characteristics,\nincluding slowed exponential-phase growth, increased turbidity in\nstationary phase, and increased colony opacity. Thin-section electron\nmicrographs showed that mutant cells did not fully separate but grew as\nclumps. Complementation of the\n                    <jats:italic>amiC<\/jats:italic>\n                    deletion mutant with\nwild-type\n                    <jats:italic>amiC<\/jats:italic>\n                    restored wild-type growth characteristics and\ntransparent colony morphology. Overexpression of\n                    <jats:italic>amiC<\/jats:italic>\n                    resulted\nin increased cell lysis, supporting AmiC's purported function as a\ngonococcal autolysin. However,\n                    <jats:italic>amiC<\/jats:italic>\n                    mutants still underwent\nautolysis in stationary phase, indicating that other gonococcal enzymes\nare also involved in this\nprocess.\n                  <\/jats:p>","DOI":"10.1128\/jb.00724-06","type":"journal-article","created":{"date-parts":[[2006,10,2]],"date-time":"2006-10-02T14:49:38Z","timestamp":1159800578000},"page":"7211-7221","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":56,"title":["AmiC Functions as an\n                    <i>N<\/i>\n                    -Acetylmuramyl-\n                    <scp>l<\/scp>\n                    -Alanine Amidase Necessaryfor Cell Separation and Can Promote Autolysis in\n                    <i>Neisseria gonorrhoeae<\/i>"],"prefix":"10.1128","volume":"188","author":[{"given":"Daniel L.","family":"Garcia","sequence":"first","affiliation":[{"name":"Department of Medical Microbiology and Immunology, University of Wisconsin School of Medicine and Public Health, Madison, Wisconsin\r53706"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joseph P.","family":"Dillard","sequence":"additional","affiliation":[{"name":"Department of Medical Microbiology and Immunology, University of Wisconsin School of Medicine and Public Health, Madison, Wisconsin\r53706"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.72.4.1914-1919.2004"},{"key":"e_1_3_2_3_2","doi-asserted-by":"crossref","first-page":"1171","DOI":"10.1046\/j.1365-2958.2003.03511.x","volume":"48","year":"2003","unstructured":"Berhardt, T. 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