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However, the molecular basis for type-specific immunity has not been fully elucidated. In this report, we produced and characterized an OspC mouse monoclonal antibody, 8C1, that recognizes native and recombinant OspC type A (OspC\n                      <jats:sub>A<\/jats:sub>\n                      ) but not OspC type B or K. Epitope mapping by hydrogen\u2013deuterium exchange mass spectrometry (HDX-MS) localized 8C1\u2019s epitope to a protruding ridge on the apex of OspC\n                      <jats:sub>A<\/jats:sub>\n                      \u03b1-helix 3 (residues 130\u2013150) previously known to be an immunodominant region of the molecule. Alanine scanning pinpointed 8C1\u2019s core binding motif to a solvent exposed patch consisting of residues K\n                      <jats:sub>141<\/jats:sub>\n                      , H\n                      <jats:sub>142<\/jats:sub>\n                      , T\n                      <jats:sub>143<\/jats:sub>\n                      , and D\n                      <jats:sub>144<\/jats:sub>\n                      . Analysis of 26 Lyme disease-positive serum samples confirmed human antibody reactivity with this region of OspC\n                      <jats:sub>A<\/jats:sub>\n                      , with residues E\n                      <jats:sub>140<\/jats:sub>\n                      and D\n                      <jats:sub>144<\/jats:sub>\n                      as being the most consequential. Our results underscore the importance of \u03b1-helix 3 as a target of type-specific epitopes on OspC\n                      <jats:sub>A<\/jats:sub>\n                      that should be taken into consideration in Lyme disease vaccine design.\n                    <\/jats:p>\n                    <jats:sec>\n                      <jats:title>IMPORTANCE<\/jats:title>\n                      <jats:p>\n                        A central challenge in the development of vaccines against Lyme disease, the most common vector-borne infection in the United States, is the antigenically variable nature of the lipoproteins displayed on the surface of the disease-causing spirochete,\n                        <jats:italic>Borreliella burgdorferi<\/jats:italic>\n                        . For example, antibodies against one type of outer surface protein C (OspC), a lipoprotein involved in\n                        <jats:italic>B. burgdorferi<\/jats:italic>\n                        transmission and early stages of infection, may have little or no cross reactivity with another seemingly closely related variant of OspC, thereby hampering the use of a single OspC type as a vaccine antigen. For the sake of vaccine design, it is critical to identify the specific epitopes on OspC that both restrict and enable cross-reactivity.\n                      <\/jats:p>\n                    <\/jats:sec>\n                  <\/jats:sec>","DOI":"10.1128\/spectrum.02883-24","type":"journal-article","created":{"date-parts":[[2025,2,14]],"date-time":"2025-02-14T09:00:31Z","timestamp":1739523631000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":2,"title":["A type-specific B-cell epitope at the apex of outer surface protein C (OspC) of the Lyme disease spirochete,\n                    <i>Borreliella burgdorferi<\/i>"],"prefix":"10.1128","volume":"13","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, Wadsworth Center, New York State Department of Health","place":["Albany, 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