{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T14:50:39Z","timestamp":1786978239768,"version":"build-2736575974"},"reference-count":46,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2015,3,19]],"date-time":"2015-03-19T00:00:00Z","timestamp":1426723200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000024","name":"Canadian Institutes of Health Research","doi-asserted-by":"publisher","award":["MOP \u2013 130273"],"award-info":[{"award-number":["MOP \u2013 130273"]}],"id":[{"id":"10.13039\/501100000024","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["MicrobiologyOpen"],"published-print":{"date-parts":[[2015,6]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    <jats:italic>Neisseria meningitidis<\/jats:italic>\n                    inhabits the human upper respiratory tract and is an important cause of sepsis and meningitis. A surface receptor comprised of transferrin\u2010binding proteins A and B (TbpA and TbpB), is responsible for acquiring iron from host transferrin. Sequence and immunological diversity divides TbpBs into two distinct lineages; isotype I and isotype II. Two representative isotype I and II strains, B16B6 and M982, differ in their dependence on TbpB for in\u00a0vitro growth on exogenous transferrin. The crystal structure of TbpB and a structural model for TbpA from the representative isotype I\n                    <jats:italic>N.\u00a0meningitidis<\/jats:italic>\n                    strain B16B6 were obtained. The structures were integrated with a comprehensive analysis of the sequence diversity of these proteins to probe for potential functional differences. A distinct isotype I TbpA was identified that co\u2010varied with TbpB and lacked sequence in the region for the loop 3\n                    <jats:italic>\u03b1<\/jats:italic>\n                    \u2010helix that is proposed to be involved in iron removal from transferrin. The tightly associated isotype I TbpBs had a distinct anchor peptide region, a distinct, smaller linker region between the lobes and lacked the large loops in the isotype II C\u2010lobe. Sequences of the intact TbpB, the TbpB N\u2010lobe, the TbpB C\u2010lobe, and TbpA were subjected to phylogenetic analyses. The phylogenetic clustering of TbpA and the TbpB C\u2010lobe were similar with two main branches comprising the isotype 1 and isotype 2 TbpBs, possibly suggesting an association between TbpA and the TbpB C\u2010lobe. The intact TbpB and TbpB N\u2010lobe had 4 main branches, one consisting of the isotype 1 TbpBs. One isotype 2 TbpB cluster appeared to consist of isotype 1 N\u2010lobe sequences and isotype 2 C\u2010lobe sequences, indicating the swapping of N\u2010lobes and C\u2010lobes. Our findings should inform future studies on the interaction between TbpB and TbpA and the process of iron acquisition.\n                  <\/jats:p>","DOI":"10.1002\/mbo3.254","type":"journal-article","created":{"date-parts":[[2015,3,20]],"date-time":"2015-03-20T11:59:50Z","timestamp":1426852790000},"page":"491-504","source":"Crossref","is-referenced-by-count":18,"title":["Patterns of structural and sequence variation within isotype lineages of the\n                    <i>Neisseria meningitidis<\/i>\n                    transferrin receptor system"],"prefix":"10.1002","volume":"4","author":[{"given":"Paul","family":"Adamiak","sequence":"first","affiliation":[{"name":"Department of Microbiology, Immunology and Infectious Diseases University of Calgary Calgary Alberta T2N 4N1 Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Charles","family":"Calmettes","sequence":"additional","affiliation":[{"name":"Department of Biochemistry University of Toronto Toronto Ontario M5S 1A8 Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Trevor F.","family":"Moraes","sequence":"additional","affiliation":[{"name":"Department of Biochemistry University of Toronto Toronto Ontario M5S 1A8 Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anthony B.","family":"Schryvers","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Immunology and Infectious Diseases University of Calgary Calgary Alberta T2N 4N1 Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2015,3,19]]},"reference":[{"key":"e_1_2_7_2_1","doi-asserted-by":"publisher","DOI":"10.1139\/o11-076"},{"issue":"7","key":"e_1_2_7_3_1","doi-asserted-by":"crossref","first-page":"2984","DOI":"10.1128\/iai.62.7.2984-2990.1994","article-title":"Immune responses in humans and animals to meningococcal transferrin\u2010binding proteins: implications for vaccine design","volume":"62","author":"Ala'Aldeen D. 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