{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T20:09:23Z","timestamp":1791230963985,"version":"4.1.0"},"reference-count":52,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2007,7,27]],"date-time":"2007-07-27T00:00:00Z","timestamp":1185494400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2007,9]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p>The extracellular polysaccharide capsule is an essential virulence factor of <jats:italic>Neisseria meningitidis<\/jats:italic>, a leading cause of severe bacterial meningitis and sepsis. Serogroup B strains, the primary disease causing isolates in Europe and America, are encapsulated in \u03b1\u20102,8 polysialic acid (polySia). The capsular polymer is synthesized from activated sialic acid by action of a membrane\u2010associated polysialyltransferase (<jats:italic>Nm<\/jats:italic>B\u2010polyST). Here we present a comprehensive characterization of <jats:italic>Nm<\/jats:italic>B\u2010polyST. Different from earlier studies, we show that membrane association is not essential for enzyme functionality. Recombinant <jats:italic>Nm<\/jats:italic>B\u2010polyST was expressed, purified and shown to synthesize long polySia chains in a non\u2010processive manner <jats:italic>in vitro<\/jats:italic>. Subsequent structure\u2013function analyses of <jats:italic>Nm<\/jats:italic>B\u2010polyST based on refined sequence alignments allowed the identification of two functional motifs in bacterial sialyltransferases. Both (D\/E\u2010D\/E\u2010G and HP motif) are highly conserved among different sialyltransferase families with otherwise little or no sequence identity. Their functional importance for enzyme catalysis and CMP\u2010Neu5Ac binding was demonstrated by mutational analysis of <jats:italic>Nm<\/jats:italic>B\u2010polyST and is emphasized by structural data available for the <jats:italic>Pasteurella multocida<\/jats:italic> sialyltransferase <jats:italic>Pm<\/jats:italic>ST1. Together our data are the first description of conserved functional elements in the highly diverse families of bacterial (poly)sialyltransferases and thus provide an advanced basis for understanding structure\u2013function relations and for phylogenetic sorting of these important enzymes.<\/jats:p>","DOI":"10.1111\/j.1365-2958.2007.05862.x","type":"journal-article","created":{"date-parts":[[2007,7,27]],"date-time":"2007-07-27T14:52:23Z","timestamp":1185547943000},"page":"1258-1275","source":"Crossref","is-referenced-by-count":72,"title":["Biochemical characterization of a <i>Neisseria meningitidis<\/i> polysialyltransferase reveals novel functional motifs in bacterial sialyltransferases"],"prefix":"10.1111","volume":"65","author":[{"given":"Friedrich","family":"Freiberger","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Heike","family":"Claus","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Almut","family":"G\u00fcnzel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Imke","family":"Oltmann\u2010Norden","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Justine","family":"Vionnet","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Martina","family":"M\u00fchlenhoff","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ulrich","family":"Vogel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Willie F.","family":"Vann","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rita","family":"Gerardy\u2010Schahn","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Katharina","family":"Stummeyer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2007,7,27]]},"reference":[{"key":"e_1_2_6_2_1","doi-asserted-by":"publisher","DOI":"10.1128\/JB.188.5.1786-1797.2006"},{"key":"e_1_2_6_3_1","doi-asserted-by":"crossref","first-page":"1926","DOI":"10.1016\/S0021-9258(19)41784-5","article-title":"Structural determination of the sialic acid polysaccharide antigens of Neisseria meningitidis serogroups B and C with carbon 13 nuclear magnetic resonance","volume":"250","author":"Bhattacharjee A.K.","year":"1975","journal-title":"J Biol Chem"},{"key":"e_1_2_6_4_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.274.7.4106"},{"key":"e_1_2_6_5_1","doi-asserted-by":"publisher","DOI":"10.1093\/glycob\/cwj016"},{"key":"e_1_2_6_6_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.274.26.18206"},{"key":"e_1_2_6_7_1","doi-asserted-by":"publisher","DOI":"10.1038\/nsmb720"},{"key":"e_1_2_6_8_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.91.24.11427"},{"key":"e_1_2_6_9_1","doi-asserted-by":"publisher","DOI":"10.1007\/PL00008618"},{"key":"e_1_2_6_10_1","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/16.22.10881"},{"key":"e_1_2_6_11_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1467-7652.2004.00062.x"},{"key":"e_1_2_6_12_1","doi-asserted-by":"publisher","DOI":"10.1128\/CMR.13.1.144"},{"key":"e_1_2_6_13_1","doi-asserted-by":"publisher","DOI":"10.1093\/glycob\/3.1.2"},{"key":"e_1_2_6_14_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.1994.tb01274.x"},{"key":"e_1_2_6_15_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00635a028"},{"issue":"3","key":"e_1_2_6_16_1","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1042\/bj2800575","article-title":"H.p.l.c. of oligo(sialic acids). 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