{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T07:30:33Z","timestamp":1761982233724,"version":"build-2065373602"},"reference-count":44,"publisher":"American Society for Microbiology","issue":"16","license":[{"start":{"date-parts":[[2014,8,15]],"date-time":"2014-08-15T00:00:00Z","timestamp":1408060800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2014,8,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Bacillus anthracis<\/jats:named-content>\n            , the causative agent of anthrax, forms an S-layer atop its peptidoglycan envelope and displays S-layer proteins and\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Bacillus<\/jats:named-content>\n            S-layer-associated (BSL) proteins with specific functions to support cell separation of vegetative bacilli and growth in infected mammalian hosts. S-layer and BSL proteins bind via the S-layer homology (SLH) domain to the pyruvylated secondary cell wall polysaccharide (SCWP) with the repeat structure [\u21924)-\u03b2-ManNAc-(1\u21924)-\u03b2-GlcNAc-(1\u21926)-\u03b1-GlcNAc-(1\u2192]\n            <jats:sub>\n              <jats:italic>n<\/jats:italic>\n            <\/jats:sub>\n            , where \u03b1-GlcNAc and \u03b2-GlcNAc are substituted with two and one galactosyl residues, respectively.\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. anthracis<\/jats:named-content>\n            <jats:italic>gneY<\/jats:italic>\n            (BAS5048) and\n            <jats:italic>gneZ<\/jats:italic>\n            (BAS5117) encode nearly identical UDP-GlcNAc 2-epimerase enzymes that catalyze the reversible conversion of UDP-GlcNAc and UDP-ManNAc. UDP-GlcNAc 2-epimerase enzymes have been shown to be required for the attachment of the phage lysin PlyG with the bacterial envelope and for bacterial growth. Here, we asked whether\n            <jats:italic>gneY<\/jats:italic>\n            and\n            <jats:italic>gneZ<\/jats:italic>\n            are required for the synthesis of the pyruvylated SCWP and for S-layer assembly. We show that\n            <jats:italic>gneZ<\/jats:italic>\n            , but not\n            <jats:italic>gneY<\/jats:italic>\n            , is required for\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. anthracis<\/jats:named-content>\n            vegetative growth, rod cell shape, S-layer assembly, and synthesis of pyruvylated SCWP. Nevertheless, inducible expression of\n            <jats:italic>gneY<\/jats:italic>\n            alleviated all the defects associated with the\n            <jats:italic>gneZ<\/jats:italic>\n            mutant. In contrast to vegetative growth, neither germination of\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. anthracis<\/jats:named-content>\n            spores nor the formation of spores in mother cells required UDP-GlcNAc 2-epimerase activity.\n          <\/jats:p>","DOI":"10.1128\/jb.01829-14","type":"journal-article","created":{"date-parts":[[2014,6,10]],"date-time":"2014-06-10T05:18:47Z","timestamp":1402377527000},"page":"2969-2978","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":15,"title":["GneZ, a UDP-GlcNAc 2-Epimerase, Is Required for S-Layer Assembly and Vegetative Growth of Bacillus anthracis"],"prefix":"10.1128","volume":"196","author":[{"given":"Ya-Ting","family":"Wang","sequence":"first","affiliation":[{"name":"Howard Taylor Ricketts Laboratory, Argonne National Laboratory, Lemont, Illinois, USA, and Department of Microbiology, University of Chicago, Chicago, Illinois, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dominique","family":"Missiakas","sequence":"additional","affiliation":[{"name":"Howard Taylor Ricketts Laboratory, Argonne National Laboratory, Lemont, Illinois, USA, and Department of Microbiology, University of Chicago, Chicago, Illinois, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Olaf","family":"Schneewind","sequence":"additional","affiliation":[{"name":"Howard Taylor Ricketts Laboratory, Argonne National Laboratory, Lemont, Illinois, USA, and Department of Microbiology, University of Chicago, Chicago, Illinois, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M605768200"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2010.06.059"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1093\/glycob\/cws080"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2008.06169.x"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M111.248070"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature01026"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0060754"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M502723200"},{"key":"e_1_3_2_10_2","doi-asserted-by":"publisher","DOI":"10.1021\/ja3069962"},{"key":"e_1_3_2_11_2","doi-asserted-by":"publisher","DOI":"10.1093\/glycob\/cwt019"},{"key":"e_1_3_2_12_2","doi-asserted-by":"publisher","DOI":"10.1038\/sj.embor.7401154"},{"key":"e_1_3_2_13_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1986.tb10469.x"},{"key":"e_1_3_2_14_2","doi-asserted-by":"crossref","first-page":"2079","DOI":"10.1099\/00221287-148-7-2079","article-title":"tagO is involved in the synthesis of all anionic cell-wall polymers in Bacillus subtilis 168","volume":"148","author":"Soldo B","year":"2002","unstructured":"SoldoBLazarevicVKaramataD. 2002. tagO is involved in the synthesis of all anionic cell-wall polymers in Bacillus subtilis 168. 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