{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,4]],"date-time":"2026-06-04T05:11:18Z","timestamp":1780549878971,"version":"3.54.1"},"reference-count":33,"publisher":"American Society for Microbiology","issue":"10","license":[{"start":{"date-parts":[[2006,10,1]],"date-time":"2006-10-01T00:00:00Z","timestamp":1159660800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Clin Vaccine Immunol"],"published-print":{"date-parts":[[2006,10]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The OspC protein of\n            <jats:italic>Borrelia burgdorferi<\/jats:italic>\n            is an immunodominant antigen. Here we demonstrate that the loop 5 domain of type A OspC is surface exposed, elicits bactericidal antibody in mice, and is antigenic in humans. The data suggest that loop 5 may be suitable for inclusion in a polyvalent, chimeric OspC vaccinogen.\n          <\/jats:p>","DOI":"10.1128\/cvi.00099-06","type":"journal-article","created":{"date-parts":[[2006,10,6]],"date-time":"2006-10-06T20:24:23Z","timestamp":1160166263000},"page":"1162-1165","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":38,"title":["Analysis of Antibody Response in Humans to the Type A OspC Loop 5 Domain and Assessment of the Potential Utility of the Loop 5 Epitope in Lyme Disease Vaccine Development"],"prefix":"10.1128","volume":"13","author":[{"given":"Eric L.","family":"Buckles","sequence":"first","affiliation":[{"name":"Department of Microbiology and Immunology"},{"name":"Center for the Study of Biological Complexity, Medical College of Virginia at Virginia Commonwealth University, Richmond, Virginia 23298-0678"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christopher G.","family":"Earnhart","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology"},{"name":"Center for the Study of Biological Complexity, Medical College of Virginia at Virginia Commonwealth University, Richmond, Virginia 23298-0678"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Richard T.","family":"Marconi","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology"},{"name":"Center for the Study of Biological Complexity, Medical College of Virginia at Virginia Commonwealth University, Richmond, Virginia 23298-0678"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/JCM.43.4.1879-1884.2005"},{"key":"e_1_3_2_3_2","doi-asserted-by":"crossref","unstructured":"Apta D. K. Raviprakashb A. Brinkman A. Semyonov S. Yang C. Skinnera L. Diehl R. Lyons K. Porter and J. Punnonen. 2006. Tetravalent neutralizing antibody response against four dengue serotypes by a single chimeric dengue envelope antigen. Vaccine 24 : 335-344.","DOI":"10.1016\/j.vaccine.2005.07.100"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1128\/iai.65.11.4661-4667.1997"},{"key":"e_1_3_2_5_2","doi-asserted-by":"crossref","unstructured":"Caro-Aguilar I. S. Lapp J. Pohl M. R. Galinski and A. Moreno. 2005. Chimeric epitopes delivered by polymeric synthetic linear peptides induce protective immunity to malaria. Microbes Infect. 7 : 1324-1337.","DOI":"10.1016\/j.micinf.2005.04.020"},{"key":"e_1_3_2_6_2","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/S0264-410X(98)00150-9","volume":"17","year":"1999","unstructured":"Dale, J. B. 1999. Mutlivalent group A streptococcal vaccine designed to optimize the immunogenicity of six tandem M protein fragments. 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