{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,9]],"date-time":"2026-03-09T23:39:13Z","timestamp":1773099553948,"version":"3.50.1"},"reference-count":56,"publisher":"American Society for Microbiology","issue":"1","license":[{"start":{"date-parts":[[2012,1,1]],"date-time":"2012-01-01T00:00:00Z","timestamp":1325376000000},"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":["Infect Immun"],"published-print":{"date-parts":[[2012,1]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Borrelia burgdorferi<\/jats:named-content>\n            , a tick-borne bacterial pathogen, causes a disseminated infection involving multiple organs known as Lyme disease. Surface proteins can directly participate in microbial virulence by facilitating pathogen dissemination via interaction with host factors. We show here that a fraction of the\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. burgdorferi<\/jats:named-content>\n            chromosomal gene product BB0337, annotated as enolase or phosphopyruvate dehydratase, is associated with spirochete outer membrane and is surface exposed.\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. burgdorferi<\/jats:named-content>\n            enolase, either in a recombinant form or as a membrane-bound native antigen, displays enzymatic activities intrinsic to the glycolytic pathway. However, the protein also interacts with host plasminogen, potentially leading to its activation and resulting in\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. burgdorferi<\/jats:named-content>\n            -induced fibrinolysis. As expected, enolase displayed consistent expression\n            <jats:italic>in vivo<\/jats:italic>\n            , however, with a variable temporal and spatial expression during spirochete infection in mice and ticks. Despite an extracellular exposure of the antigen and a potential role in host-pathogen interaction, active immunization of mice with recombinant enolase failed to evoke protective immunity against subsequent\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. burgdorferi<\/jats:named-content>\n            infection. In contrast, enolase immunization of murine hosts significantly reduced the acquisition of spirochetes by feeding ticks, suggesting that the protein could have a stage-specific role in\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. burgdorferi<\/jats:named-content>\n            survival in the feeding vector. Strategies to interfere with the function of surface enolase could contribute to the development of novel preventive measures to interrupt the spirochete infection cycle and reduce the incidences of Lyme disease.\n          <\/jats:p>","DOI":"10.1128\/iai.05671-11","type":"journal-article","created":{"date-parts":[[2011,10,25]],"date-time":"2011-10-25T02:21:28Z","timestamp":1319509288000},"page":"82-90","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":58,"title":["A Surface Enolase Participates in Borrelia burgdorferi-Plasminogen Interaction and Contributes to Pathogen Survival within Feeding Ticks"],"prefix":"10.1128","volume":"80","author":[{"given":"Sarah Veloso","family":"Nogueira","sequence":"first","affiliation":[{"name":"Department of Veterinary Medicine, University of Maryland, College Park, Maryland 20742, USA, and Virginia-Maryland Regional College of Veterinary Medicine, College Park, Maryland 20742, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alexis A.","family":"Smith","sequence":"additional","affiliation":[{"name":"Department of Veterinary Medicine, University of Maryland, College Park, Maryland 20742, USA, and Virginia-Maryland Regional College of Veterinary Medicine, College Park, Maryland 20742, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jin-Hong","family":"Qin","sequence":"additional","affiliation":[{"name":"Department of Veterinary Medicine, University of Maryland, College Park, Maryland 20742, USA, and Virginia-Maryland Regional College of Veterinary Medicine, College Park, Maryland 20742, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Utpal","family":"Pal","sequence":"additional","affiliation":[{"name":"Department of Veterinary Medicine, University of Maryland, College Park, Maryland 20742, USA, and Virginia-Maryland Regional College of Veterinary Medicine, College Park, Maryland 20742, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbapap.2008.03.017"},{"key":"e_1_3_2_3_2","first-page":"353","volume-title":"Borrelia, molecular biology, host interaction and pathogenesis","author":"Barthold SW","year":"2010","unstructured":"BartholdSWDiegoCPhilippMT. 2010. 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