{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,19]],"date-time":"2026-09-19T20:39:44Z","timestamp":1789850384595,"version":"4.0.1"},"reference-count":40,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2016,1,5]],"date-time":"2016-01-05T00:00:00Z","timestamp":1451952000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2016,1,5]],"date-time":"2016-01-05T00:00:00Z","timestamp":1451952000000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/501100000837","name":"University of Nottingham","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000837","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["MicrobiologyOpen"],"published-print":{"date-parts":[[2016,4]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    <jats:italic>Neisseria meningitidis<\/jats:italic>\n                    is a leading cause of fatal sepsis and meningitis worldwide. As for commensal species of human neisseriae,\n                    <jats:italic>N. meningitidis<\/jats:italic>\n                    inhabits the human nasopharynx and asymptomatic colonization is ubiquitous. Only rarely does the organism invade and survive in the bloodstream leading to disease. Moonlighting proteins perform two or more autonomous, often dissimilar, functions using a single polypeptide chain. They have been increasingly reported on the surface of both prokaryotic and eukaryotic organisms and shown to interact with a variety of host ligands. In some organisms moonlighting proteins perform virulence\u2010related functions, and they may play a role in the pathogenesis of\n                    <jats:italic>N. meningitidis<\/jats:italic>\n                    . Fructose\u20101,6\u2010bisphosphate aldolase (FBA) was previously shown to be surface\u2010exposed in meningococci and involved in adhesion to host cells. In this study, FBA was shown to be present on the surface of both pathogenic and commensal neisseriae, and surface localization and anchoring was demonstrated to be independent of aldolase activity. Importantly, meningococcal FBA was found to bind to human glu\u2010plasminogen in a dose\u2010dependent manner. Site\u2010directed mutagenesis demonstrated that the C\u2010terminal lysine residue of FBA was required for this interaction, whereas subterminal lysine residues were not involved.\n                  <\/jats:p>","DOI":"10.1002\/mbo3.331","type":"journal-article","created":{"date-parts":[[2016,1,5]],"date-time":"2016-01-05T20:12:45Z","timestamp":1452024765000},"page":"340-350","source":"Crossref","is-referenced-by-count":17,"title":["Fructose\u20101,6\u2010bisphosphate aldolase of\n                    <i>Neisseria meningitidis<\/i>\n                    binds human plasminogen via its C\u2010terminal lysine residue"],"prefix":"10.1002","volume":"5","author":[{"given":"Fariza","family":"Shams","sequence":"first","affiliation":[{"name":"School of Life Sciences Molecular Bacteriology and Immunology Group Centre for Biomolecular Sciences University of Nottingham Nottingham NG7 2RD United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Neil J.","family":"Oldfield","sequence":"additional","affiliation":[{"name":"School of Life Sciences Molecular Bacteriology and Immunology Group Centre for Biomolecular Sciences University of Nottingham Nottingham NG7 2RD United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Si Kei","family":"Lai","sequence":"additional","affiliation":[{"name":"School of Life Sciences Molecular Bacteriology and Immunology Group Centre for Biomolecular Sciences University of Nottingham Nottingham NG7 2RD United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sarfraz A.","family":"Tunio","sequence":"additional","affiliation":[{"name":"School of Life Sciences Molecular Bacteriology and Immunology Group Centre for Biomolecular Sciences University of Nottingham Nottingham NG7 2RD United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karl G.","family":"Wooldridge","sequence":"additional","affiliation":[{"name":"School of Life Sciences Molecular Bacteriology and Immunology Group Centre for Biomolecular Sciences University of Nottingham Nottingham NG7 2RD United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David P. 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