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Although many surface-localized glycoproteins have been identified in bacterial pathogens and symbionts, it not clear if and how selection impacts associated glycoform structure. Here, a systematic approach was devised to correlate gene repertoire with protein-associated glycoform structure in<jats:italic>Neisseria<\/jats:italic>species important to human health and disease. By manipulating the protein glycosylation (<jats:italic>pgl<\/jats:italic>) gene content and assessing the glycan structure by mass spectrometry and reactivity with monoclonal antibodies, it was established that protein-associated glycans are antigenically variable and that at least nine distinct glycoforms can be expressed<jats:italic>in vitro<\/jats:italic>. These studies also revealed that in addition to<jats:italic>Neisseria gonorrhoeae<\/jats:italic>strain N400, one other gonococcal strain and isolates of<jats:italic>Neisseria meningitidis<\/jats:italic>and<jats:italic>Neisseria lactamica<\/jats:italic>exhibit broad-spectrum O-linked protein glycosylation. Although a strong correlation between<jats:italic>pgl<\/jats:italic>gene content, glycoform expression, and serological profile was observed, there were significant exceptions, particularly with regard to levels of microheterogeneity. This work provides a technological platform for molecular serotyping of neisserial protein glycans and for elucidating<jats:italic>pgl<\/jats:italic>gene evolution.<\/jats:p>","DOI":"10.1128\/jb.00101-10","type":"journal-article","created":{"date-parts":[[2010,4,3]],"date-time":"2010-04-03T00:56:37Z","timestamp":1270256197000},"page":"2816-2829","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":54,"title":["Genetic, Structural, and Antigenic Analyses of Glycan Diversity in the O-Linked Protein Glycosylation Systems of Human<i>Neisseria<\/i>Species"],"prefix":"10.1128","volume":"192","author":[{"given":"Bente","family":"B\u00f8rud","sequence":"first","affiliation":[{"name":"Centre for Molecular Biology and Neuroscience"},{"name":"Department of Molecular Biosciences"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Finn Erik","family":"Aas","sequence":"additional","affiliation":[{"name":"Centre for Molecular Biology and Neuroscience"},{"name":"Department of Molecular Biosciences"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"A\u030ashild","family":"Vik","sequence":"additional","affiliation":[{"name":"Centre for Molecular Biology and Neuroscience"},{"name":"Department of Molecular Biosciences"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hanne C.","family":"Winther-Larsen","sequence":"additional","affiliation":[{"name":"Centre for Molecular Biology and Neuroscience"},{"name":"Department of Molecular Biosciences"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wolfgang","family":"Egge-Jacobsen","sequence":"additional","affiliation":[{"name":"Centre for Molecular Biology and Neuroscience"},{"name":"Department of Molecular Biosciences"},{"name":"Glyconor Mass Spectrometry &amp; Proteomics Unit, University of Oslo, 0316 Oslo, Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael","family":"Koomey","sequence":"additional","affiliation":[{"name":"Centre for Molecular Biology and Neuroscience"},{"name":"Department of Molecular Biosciences"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"crossref","first-page":"27712","DOI":"10.1074\/jbc.M604324200","volume":"281","year":"2006","unstructured":"Aas, F. 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