{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,21]],"date-time":"2026-09-21T06:02:46Z","timestamp":1789970566144,"version":"4.0.1"},"reference-count":61,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2026,9,21]],"date-time":"2026-09-21T00:00:00Z","timestamp":1789948800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Immunol."],"abstract":"<jats:sec>\n                    <jats:title>Introduction<\/jats:title>\n                    <jats:p>\n                      Shigellosis morbidity and mortality, combined with the increase in multidrug-resistant infections, make\n                      <jats:italic>Shigella<\/jats:italic>\n                      vaccine development a global imperative. Glycoconjugate vaccines that couple immunogenic O-antigen to protein derived from\n                      <jats:italic>Shigella<\/jats:italic>\n                      may provide broader protection across\n                      <jats:italic>Shigella<\/jats:italic>\n                      species and serogroups. Such an approach also circumvents immunotolerance arising from repeated use of the same carrier. Here we use bioconjugation, exploiting an oligosaccharyltransferase (OST) enzyme to couple O-antigen and carrier protein\n                      <jats:italic>in vivo<\/jats:italic>\n                      , to generate a\n                      <jats:italic>Shigella<\/jats:italic>\n                      -specific dual-target glycoconjugate.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Methods<\/jats:title>\n                    <jats:p>\n                      Glycoconjugates were synthesised in\n                      <jats:italic>E. coli<\/jats:italic>\n                      SDB1 cells producing\n                      <jats:italic>S. sonnei<\/jats:italic>\n                      O-antigen, the OST PglS, and one of two\n                      <jats:italic>Shigella<\/jats:italic>\n                      carrier proteins or the standard bioconjugate carrier, ExoA. Recombinant glycoconjugate was purified using anion exchange chromatography and then used to immunise mice. Antibody responses were measured and compared by ELISA.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>\n                      When co-produced in\n                      <jats:italic>E. coli<\/jats:italic>\n                      , PglS was able to transfer the cloned\n                      <jats:italic>S. sonnei<\/jats:italic>\n                      O-antigen onto three carrier proteins, modified to accept glycans from the PglS transferase enzyme\u2014ExoA and two immunogenic\n                      <jats:italic>Shigella<\/jats:italic>\n                      -specific outer membrane proteins, EmrK and MdtA. Production of MdtA or ExoA glycoconjugates for immunisation studies utilised successive rounds of anion exchange chromatography, to remove unglycosylated material and obtain highly purified glycosylated proteins. Analysis of murine sera following immunisation revealed an IgG response was raised against both carrier protein and the\n                      <jats:italic>S. sonnei<\/jats:italic>\n                      O-antigen for each glycoconjugate.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Discussion<\/jats:title>\n                    <jats:p>\n                      A novel, conserved\n                      <jats:italic>Shigella<\/jats:italic>\n                      protein can be utilised as an effective carrier for the\n                      <jats:italic>S. sonnei<\/jats:italic>\n                      O-antigen to generate a\n                      <jats:italic>Shigella<\/jats:italic>\n                      -specific glycoconjugate that elicits IgG responses to both carrier protein and\n                      <jats:italic>S. sonnei<\/jats:italic>\n                      O-antigen.\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.3389\/fimmu.2026.1907725","type":"journal-article","created":{"date-parts":[[2026,9,21]],"date-time":"2026-09-21T05:35:29Z","timestamp":1789968929000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":0,"title":["Development and evaluation of a dual-target glycoconjugate against Shigella sonnei"],"prefix":"10.3389","volume":"17","author":[{"given":"Catherine L.","family":"Hall","sequence":"first","affiliation":[{"name":"Department of Infection Biology, Faculty of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine","place":["London, United Kingdom"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tom L.","family":"Flood","sequence":"additional","affiliation":[{"name":"Department of Infection Biology, Faculty of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine","place":["London, United 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