{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,26]],"date-time":"2026-10-26T17:28:58Z","timestamp":1793035738589,"version":"4.5.0"},"reference-count":58,"publisher":"American Society for Microbiology","issue":"4","license":[{"start":{"date-parts":[[2024,4,9]],"date-time":"2024-04-09T00:00:00Z","timestamp":1712620800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/doi.org\/10.1128\/ASMCopyrightv2"},{"start":{"date-parts":[[2024,4,9]],"date-time":"2024-04-09T00:00:00Z","timestamp":1712620800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/100000060","name":"HHS | NIH | National Institute of Allergy and Infectious Diseases","doi-asserted-by":"crossref","award":["75N93019C00040"],"award-info":[{"award-number":["75N93019C00040"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Infect Immun"],"published-print":{"date-parts":[[2024,4,9]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:sec>\n                    <jats:title\/>\n                    <jats:p>\n                      Camelid-derived, single-domain antibodies (V\n                      <jats:sub>H<\/jats:sub>\n                      Hs) have proven to be extremely powerful tools in defining the antigenic landscape of immunologically heterogeneous surface proteins. In this report, we generated a phage-displayed V\n                      <jats:sub>H<\/jats:sub>\n                      H library directed against the candidate Lyme disease vaccine antigen, outer surface protein A (OspA). Two alpacas were immunized with recombinant OspA serotype 1 from\n                      <jats:italic>Borrelia burgdorferi sensu stricto<\/jats:italic>\n                      strain B31, in combination with the canine vaccine RECOMBITEK Lyme containing lipidated OspA. The phage library was subjected to two rounds of affinity enrichment (\u201cpanning\u201d) against recombinant OspA, yielding 21 unique V\n                      <jats:sub>H<\/jats:sub>\n                      Hs within two epitope bins, as determined through competition enzyme linked immunosorbent assays (ELISAs) with a panel of OspA-specific human monoclonal antibodies. Epitope refinement was conducted by hydrogen exchange-mass spectrometry. Six of the monovalent V\n                      <jats:sub>H<\/jats:sub>\n                      Hs were expressed as human IgG1-Fc fusion proteins and shown to have functional properties associated with protective human monoclonal antibodies, including\n                      <jats:italic>B. burgdorferi<\/jats:italic>\n                      agglutination, outer membrane damage, and complement-dependent borreliacidal activity. The V\n                      <jats:sub>H<\/jats:sub>\n                      Hs displayed unique reactivity profiles with the seven OspA serotypes associated with\n                      <jats:italic>B. burgdorferi<\/jats:italic>\n                      genospecies in the United States and Europe consistent with there being unique epitopes across OspA serotypes that should be considered when designing and evaluating multivalent Lyme disease vaccines.\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1128\/iai.00084-24","type":"journal-article","created":{"date-parts":[[2024,3,17]],"date-time":"2024-03-17T13:21:19Z","timestamp":1710681679000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":14,"title":["Single-domain antibodies reveal unique borrelicidal epitopes on the Lyme disease vaccine antigen, outer surface protein A (OspA)"],"prefix":"10.1128","volume":"92","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-9913-7722","authenticated-orcid":false,"given":"David J.","family":"Vance","sequence":"first","affiliation":[{"name":"Division of Infectious Diseases, New York State Department of Health, Wadsworth Center, Albany, New York, USA"},{"name":"Department of Biomedical Sciences, University at Albany, Albany, New York, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Saiful","family":"Basir","sequence":"additional","affiliation":[{"name":"Department of Biomedical Sciences, University at Albany, Albany, New York, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carol Lyn","family":"Piazza","sequence":"additional","affiliation":[{"name":"Division of Infectious Diseases, New York State Department of Health, Wadsworth Center, Albany, New York, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Graham G.","family":"Willsey","sequence":"additional","affiliation":[{"name":"Division of Infectious Diseases, New York State Department of Health, Wadsworth Center, Albany, New York, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"H. M. Emranul","family":"Haque","sequence":"additional","affiliation":[{"name":"Department of Chemistry, The University of Kansas, Lawrence, Kansas, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jacque M.","family":"Tremblay","sequence":"additional","affiliation":[{"name":"Department of Infectious Disease and Global Health, Cummings School of Veterinary Medicine, Tufts University, North Grafton, Massachusetts, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael J.","family":"Rudolph","sequence":"additional","affiliation":[{"name":"New York Structural Biology Center, New York, New York, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Beatrice","family":"Muriuki","sequence":"additional","affiliation":[{"name":"Department of Medicine, University of Massachusetts Chan School of Medicine, Worcester, Massachusetts, 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