{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T02:54:11Z","timestamp":1792032851695,"version":"4.4.0"},"reference-count":30,"publisher":"American Society for Microbiology","issue":"19","license":[{"start":{"date-parts":[[2010,10,1]],"date-time":"2010-10-01T00:00:00Z","timestamp":1285891200000},"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":[[2010,10]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            <jats:italic>Bacillus anthracis<\/jats:italic>\n            spores, the etiological agents of anthrax, possess a loosely fitting outer layer called the exosporium that is composed of a basal layer and an external hairlike nap. The filaments of the nap are formed by trimers of the collagenlike glycoprotein BclA. Multiple pentasaccharide and trisaccharide side chains are O linked to BclA. The nonreducing terminal residue of the pentasaccharide side chain is the unusual sugar anthrose. A plausible biosynthetic pathway for anthrose biosynthesis has been proposed, and an\n            <jats:italic>antABCD<\/jats:italic>\n            operon encoding four putative anthrose biosynthetic enzymes has been identified. In this study, we genetically and biochemically characterized the activities of these enzymes. We also used mutant\n            <jats:italic>B. anthracis<\/jats:italic>\n            strains to determine the effects on BclA glycosylation of individually inactivating the genes of the anthrose operon. The inactivation of\n            <jats:italic>antA<\/jats:italic>\n            resulted in the appearance of BclA pentasaccharides containing anthrose analogs possessing shorter side chains linked to the amino group of the sugar. The inactivation of\n            <jats:italic>antB<\/jats:italic>\n            resulted in BclA being replaced with only trisaccharides, suggesting that the enzyme encoded by the gene is a dTDP-\u03b2-\n            <jats:sc>l<\/jats:sc>\n            -rhamnose \u03b1-1,3-\n            <jats:sc>l<\/jats:sc>\n            -rhamnosyl transferase that attaches the fourth residue of the pentasaccharide side chain. The inactivation of\n            <jats:italic>antC<\/jats:italic>\n            and\n            <jats:italic>antD<\/jats:italic>\n            resulted in the disappearance of BclA pentasaccharides and the appearance of a tetrasaccharide lacking anthrose. These phenotypes are entirely consistent with the proposed roles for the\n            <jats:italic>antABCD<\/jats:italic>\n            -encoded enzymes in anthrose biosynthesis. Purified AntA was then shown to exhibit \u03b2-methylcrotonyl-coenzyme A (CoA) hydratase activity, as we predicted. Similarly, we confirmed that purified AntC had aminotransferase activity and that purified AntD displayed\n            <jats:italic>N<\/jats:italic>\n            -acyltransferase activity.\n          <\/jats:p>","DOI":"10.1128\/jb.00568-10","type":"journal-article","created":{"date-parts":[[2010,7,31]],"date-time":"2010-07-31T01:45:04Z","timestamp":1280540704000},"page":"5053-5062","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":37,"title":["Characterization of the Enzymes Encoded by the Anthrose Biosynthetic Operon of\n            <i>Bacillus anthracis<\/i>"],"prefix":"10.1128","volume":"192","author":[{"given":"Shengli","family":"Dong","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Molecular Genetics"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sylvia A.","family":"McPherson","sequence":"additional","affiliation":[{"name":"Department of Microbiology"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yun","family":"Wang","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of Alabama at Birmingham, Birmingham, Alabama 35294"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mei","family":"Li","sequence":"additional","affiliation":[{"name":"Department of Microbiology"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pengfei","family":"Wang","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of Alabama at Birmingham, Birmingham, Alabama 35294"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"suffix":"Jr.","given":"Charles L.","family":"Turnbough","sequence":"additional","affiliation":[{"name":"Department of Microbiology"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David G.","family":"Pritchard","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Genetics"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"crossref","first-page":"947","DOI":"10.1111\/j.1365-2958.2008.06206.x","volume":"68","year":"2008","unstructured":"Ball, D. A., R. Taylor, S. J. Todd, C. Redmond, E. Couture-Tosi, P. Sylvestre, A. Moir, and P. A. Bullough. 2008. Structure of the exosporium and sublayers of spores of the Bacillus cereus family revealed by electron crystallography. Mol. Microbiol. 68 : 947-958.","journal-title":"Mol. Microbiol."},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.187.15.5310-5317.2005"},{"key":"e_1_3_2_4_2","doi-asserted-by":"crossref","first-page":"30945","DOI":"10.1074\/jbc.M401613200","volume":"279","year":"2004","unstructured":"Daubenspeck, J. M., H. Zeng, P. Chen, S. Dong, C. T. Steichen, N. R. Krishna, D. G. Pritchard, and C. L. Turnbough, Jr. 2004. Novel oligosaccharide side chains of the collagen-like region of BclA, the major glycoprotein of the Bacillus anthracis exosporium. J. Biol. Chem. 279 : 30945-30953.","journal-title":"J. Biol. 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