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Interestingly, there is an unusual occurrence of 10 putative polysaccharide deacetylases, including five <jats:styled-content style=\"fixed-case\">PGNG<\/jats:styled-content>\u2010dacs, in the <jats:italic><jats:styled-content style=\"fixed-case\">B<\/jats:styled-content>acillus<\/jats:italic> sp. genomes, especially <jats:italic><jats:styled-content style=\"fixed-case\">B<\/jats:styled-content>.\u2009cereus<\/jats:italic> and <jats:italic><jats:styled-content style=\"fixed-case\">B<\/jats:styled-content>.\u2009anthracis<\/jats:italic>. To elucidate the physiological role of these multiple deacetylases, we employed genetic analysis and protein localization studies of five putative <jats:styled-content style=\"fixed-case\">PGNG<\/jats:styled-content>\u2010dacs from <jats:italic><jats:styled-content style=\"fixed-case\">B<\/jats:styled-content>.\u2009anthracis<\/jats:italic> as well as biochemical analysis of their corresponding homologues from <jats:italic><jats:styled-content style=\"fixed-case\">B<\/jats:styled-content>.\u2009cereus<\/jats:italic>. Our data confirm that three enzymes are <jats:styled-content style=\"fixed-case\">PGNG<\/jats:styled-content>\u2010dacs. While <jats:styled-content style=\"fixed-case\">BA<\/jats:styled-content>1977, associated with lateral peptidoglycan synthesis, is a <jats:italic>bona fide<\/jats:italic> peptidoglycan deacetylase involved in resistance to host lysozyme and required for full virulence, <jats:styled-content style=\"fixed-case\">BA<\/jats:styled-content>1961 and <jats:styled-content style=\"fixed-case\">BA<\/jats:styled-content>3679 participate in the biogenesis of the peptidoglycan during both elongation and cell division. Furthermore, two enzymes are important for neutral polysaccharide attachment to <jats:styled-content style=\"fixed-case\">PG<\/jats:styled-content> and consequently anchoring of <jats:styled-content style=\"fixed-case\">S<\/jats:styled-content>\u2010layer proteins (<jats:styled-content style=\"fixed-case\">BA<\/jats:styled-content>5436) and for polysaccharide modification (<jats:styled-content style=\"fixed-case\">BA<\/jats:styled-content>2944). Our results provide novel and fundamental insights into the function of polysaccharide deacetylases in a major bioterrorism agent.<\/jats:p>","DOI":"10.1111\/mmi.12137","type":"journal-article","created":{"date-parts":[[2013,1,22]],"date-time":"2013-01-22T02:36:44Z","timestamp":1358822204000},"page":"867-883","source":"Crossref","is-referenced-by-count":47,"title":["Distinct functions of polysaccharide deacetylases in cell shape, neutral polysaccharide synthesis and virulence of <i><scp>B<\/scp>acillus anthracis<\/i>"],"prefix":"10.1111","volume":"87","author":[{"given":"Stavroula","family":"Balomenou","sequence":"first","affiliation":[{"name":"Department of Biology Enzyme Biotechnology Group University of Crete  PO Box 2208, Vasilika Vouton 714 09 Heraklion, Crete Greece"},{"name":"Institute of Molecular Biology and Biotechnology  70013 Heraklion Crete Greece"},{"name":"Institut Pasteur Groupe Biologie et g\u00e9n\u00e9tique de la paroi bact\u00e9rienne  75724 Paris 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