{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,15]],"date-time":"2026-09-15T09:51:00Z","timestamp":1789465860168,"version":"build-2803163510"},"reference-count":34,"publisher":"American Society for Microbiology","issue":"7","license":[{"start":{"date-parts":[[2011,4,1]],"date-time":"2011-04-01T00:00:00Z","timestamp":1301616000000},"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":[[2011,4]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Vaccines against\n            <jats:italic>Neisseria meningitidis<\/jats:italic>\n            group C are based on its \u03b1-2,9-linked polysialic acid capsular polysaccharide. This polysialic acid expressed on the surface of\n            <jats:italic>N. meningitidis<\/jats:italic>\n            and in the absence of specific antibody serves to evade host defense mechanisms. The polysialyltransferase (PST) that forms the group C polysialic acid (NmC PST) is located in the cytoplasmic membrane. Until recently, detailed characterization of bacterial polysialyltransferases has been hampered by a lack of availability of soluble enzyme preparations. We have constructed chimeras of the group C polysialyltransferase that catalyzes the formation \u03b1-2,9-polysialic acid as a soluble enzyme. We used site-directed mutagenesis to determine the region of the enzyme necessary for synthesis of the \u03b1-2,9 linkage. A chimera of NmB and NmC PSTs containing only amino acids 1 to 107 of the NmB polysialyltransferase catalyzed the synthesis of \u03b1-2,8-polysialic acid. The NmC polysialyltransferase requires an exogenous acceptor for catalytic activity. While it requires a minimum of a disialylated oligosaccharide to catalyze transfer, it can form high-molecular-weight \u03b1-2,9-polysialic acid in a nonprocessive fashion when initiated with an \u03b1-2,8-polysialic acid acceptor.\n            <jats:italic>De novo<\/jats:italic>\n            synthesis\n            <jats:italic>in vivo<\/jats:italic>\n            requires an endogenous acceptor. We attempted to reconstitute\n            <jats:italic>de novo<\/jats:italic>\n            activity of the soluble group C polysialyltransferase with membrane components. We found that an acapsular mutant with a defect in the polysialyltransferase produces outer membrane vesicles containing an acceptor for the \u03b1-2,9-polysialyltransferase. This acceptor is an amphipathic molecule and can be elongated to produce polysialic acid that is reactive with group C-specific antibody.\n          <\/jats:p>","DOI":"10.1128\/jb.00924-10","type":"journal-article","created":{"date-parts":[[2011,1,29]],"date-time":"2011-01-29T05:23:14Z","timestamp":1296278594000},"page":"1576-1582","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":26,"title":["Characterization and Acceptor Preference of a Soluble Meningococcal Group C Polysialyltransferase"],"prefix":"10.1128","volume":"193","author":[{"given":"Dwight C.","family":"Peterson","sequence":"first","affiliation":[{"name":"Laboratory of Bacterial Polysaccharides, Center for Biologics Evaluation and Research, Bethesda, Maryland 20892"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gayathri","family":"Arakere","sequence":"additional","affiliation":[{"name":"Sir Dorabji Tata Centre for Research in Tropical Diseases, Indian Institute of Science, Bangalore, India 560012"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Justine","family":"Vionnet","sequence":"additional","affiliation":[{"name":"Laboratory of Bacterial Polysaccharides, Center for Biologics Evaluation and Research, Bethesda, Maryland 20892"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pumtiwitt C.","family":"McCarthy","sequence":"additional","affiliation":[{"name":"Laboratory of Bacterial Polysaccharides, Center for Biologics Evaluation and Research, Bethesda, Maryland 20892"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Willie F.","family":"Vann","sequence":"additional","affiliation":[{"name":"Laboratory of Bacterial Polysaccharides, Center for Biologics Evaluation and Research, Bethesda, Maryland 20892"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.188.5.1786-1797.2006"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.176.3.691-695.1994"},{"key":"e_1_3_3_4_2","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1038\/nrd3012","volume":"9","year":"2010","unstructured":"Astronomo, R. 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