{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,8]],"date-time":"2026-10-08T22:43:59Z","timestamp":1791499439981,"version":"4.3.4"},"reference-count":32,"publisher":"Wiley","issue":"10","license":[{"start":{"date-parts":[[2017,9,13]],"date-time":"2017-09-13T00:00:00Z","timestamp":1505260800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["NFP0076894"],"award-info":[{"award-number":["NFP0076894"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2017,10]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Polyvalent antigen display is an effective strategy to enhance the immunogenicity of subunit vaccines by clustering them in an array\u2010like manner on a scaffold system. This strategy results in a higher local density of antigens, increased high avidity interactions with B cells and other antigen presenting cells, and therefore a more effective presentation of vaccine antigens. In this study, we used lumazine synthase (LS), an icosahedral symmetry capsid derived from <jats:italic>Bacillus anthracis<\/jats:italic>, as a scaffold to present 60 copies of a linear B cell epitope (PB10) from the ricin toxin fused to the C terminus of LS via four different linkers. We then investigated the effects of linker length, linker rigidity and formaldehyde crosslinking on the protein assembly, conformational integrity, thermal stability, <jats:italic>in vitro<\/jats:italic> antibody binding, and immunogenicity in mice. Fusion of the PB10 peptide onto LS, with varying linker lengths, did not affect protein assembly, thermal stability or exposure of the epitope, but had a minor impact on protein conformation. Formaldehyde crosslinking considerably improved protein thermal stability with only minor impact on protein conformation. All LS_PB10 constructs, when administered to mice by injection without adjuvant, elicited measurable anti\u2010ricin serum IgG titers, although the titers were not sufficient to confer protection against a 10\u00d7 lethal dose ricin challenge. This work sheds light on the biophysical properties, immunogenicity and potential feasibility of LS from <jats:italic>B. anthracis<\/jats:italic> as a scaffold system for polyvalent antigen display.<\/jats:p>","DOI":"10.1002\/pro.3243","type":"journal-article","created":{"date-parts":[[2017,7,24]],"date-time":"2017-07-24T08:28:37Z","timestamp":1500884917000},"page":"2059-2072","source":"Crossref","is-referenced-by-count":17,"title":["Evaluation of lumazine synthase from <i>Bacillus anthracis<\/i> as a presentation platform for polyvalent antigen display"],"prefix":"10.1002","volume":"26","author":[{"given":"Yangjie","family":"Wei","sequence":"first","affiliation":[{"name":"Macromolecule and Vaccine Stabilization Center Department of Pharmaceutical Chemistry, University of Kansas Lawrence Kansas 66047"},{"name":"Department of Pharmaceutical Chemistry University of Kansas Lawrence Kansas 66047"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Newton","family":"Wahome","sequence":"additional","affiliation":[{"name":"Macromolecule and Vaccine Stabilization Center Department of Pharmaceutical Chemistry, University of Kansas Lawrence Kansas 66047"},{"name":"Department of Pharmaceutical Chemistry University of Kansas Lawrence Kansas 66047"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Greta","family":"VanSlyke","sequence":"additional","affiliation":[{"name":"Division of Infectious Disease Wadsworth Center, New York State Department of Health Albany New York 12208"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Neal","family":"Whitaker","sequence":"additional","affiliation":[{"name":"Macromolecule and Vaccine Stabilization Center Department of Pharmaceutical Chemistry, University of Kansas Lawrence Kansas 66047"},{"name":"Department of Pharmaceutical Chemistry University of Kansas Lawrence Kansas 66047"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Prashant","family":"Kumar","sequence":"additional","affiliation":[{"name":"Macromolecule and Vaccine Stabilization Center Department of Pharmaceutical Chemistry, University of Kansas Lawrence Kansas 66047"},{"name":"Division of Infectious Disease Wadsworth Center, New York State Department of Health Albany New York 12208"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael L.","family":"Barta","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Chemistry University of Kansas Lawrence Kansas 66047"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wendy L.","family":"Picking","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Chemistry University of Kansas Lawrence Kansas 66047"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David B.","family":"Volkin","sequence":"additional","affiliation":[{"name":"Macromolecule and Vaccine Stabilization Center Department of Pharmaceutical Chemistry, University of Kansas Lawrence Kansas 66047"},{"name":"Department of Pharmaceutical Chemistry University of Kansas Lawrence Kansas 66047"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nicholas J.","family":"Mantis","sequence":"additional","affiliation":[{"name":"Division of Infectious Disease Wadsworth Center, New York State Department of Health Albany New York 12208"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C. Russell","family":"Middaugh","sequence":"additional","affiliation":[{"name":"Macromolecule and Vaccine Stabilization Center Department of Pharmaceutical Chemistry, University of Kansas Lawrence Kansas 66047"},{"name":"Department of Pharmaceutical Chemistry University of Kansas Lawrence Kansas 66047"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2017,9,13]]},"reference":[{"key":"e_1_2_6_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.bcp.2016.05.001"},{"key":"e_1_2_6_3_1","doi-asserted-by":"publisher","DOI":"10.1101\/cshperspect.a002295"},{"key":"e_1_2_6_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jsb.2003.08.004"},{"key":"e_1_2_6_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.addr.2014.10.023"},{"key":"e_1_2_6_6_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.vaccine.2013.11.069"},{"key":"e_1_2_6_7_1","first-page":"437","volume-title":"Production of well\u2010characterized virus\u2010like particles in an escherichia coli\u2010based expression platform for preclinical vaccine assessments","author":"Wahome N","year":"2016"},{"key":"e_1_2_6_8_1","doi-asserted-by":"publisher","DOI":"10.1111\/febs.12255"},{"key":"e_1_2_6_9_1","doi-asserted-by":"publisher","DOI":"10.1039\/C4RA10187A"},{"key":"e_1_2_6_10_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.1234150"},{"key":"e_1_2_6_11_1","first-page":"1001","article-title":"Structural study and thermodynamic characterization of inhibitor binding to lumazine synthase from bacillus anthracis","volume":"66","author":"Morgunova E","year":"2010","journal-title":"Acta Cryst"},{"key":"e_1_2_6_12_1","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.2000.4435"},{"key":"e_1_2_6_13_1","doi-asserted-by":"publisher","DOI":"10.1001\/jama.294.18.2342"},{"key":"e_1_2_6_14_1","doi-asserted-by":"publisher","DOI":"10.4161\/hv.24063"},{"key":"e_1_2_6_15_1","doi-asserted-by":"crossref","unstructured":"Roxas\u2010DuncanVI SmithLA Progress in the development of vaccines against ricin intoxication. 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