{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,1]],"date-time":"2026-11-01T04:17:40Z","timestamp":1793506660545,"version":"4.5.0"},"reference-count":28,"publisher":"American Society for Microbiology","issue":"7","license":[{"start":{"date-parts":[[2008,7,1]],"date-time":"2008-07-01T00:00:00Z","timestamp":1214870400000},"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":[[2008,7]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:p>Despite effective chemotherapy, schistosomiasis remains a major public health problem in the developing world, with at least 200 million active infections resulting in significant morbidity. Rapid reinfection after treatment, accompanied by extensive residual morbidity, mandates alternative control strategies, including vaccine development. Paramyosin, a myofibrillar protein found only in invertebrates, has been widely studied as a vaccine candidate for both<jats:italic>Schistosoma mansoni<\/jats:italic>and<jats:italic>Schistosoma japonicum<\/jats:italic>. Recently, we demonstrated that Th2-biased immune responses to paramyosin are associated with resistance to reinfection with<jats:italic>S. japonicum<\/jats:italic>in humans; however, challenges in the pilot-scale production of schistosome paramyosin have hampered further studies of this promising vaccine candidate. Here we report a method for the pilot-scale expression and purification of recombinant<jats:italic>S. japonicum<\/jats:italic>paramyosin (rSj97). rSj97 was extracted from<jats:italic>Escherichia coli<\/jats:italic>inclusion bodies and purified with sequential anion-exchange, hydroxyapatite, and size exclusion chromatography. The purified rSj97 was &gt;95% pure as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoretic analysis and was free of significant endotoxin contamination. We demonstrate that, like native paramyosin, rSj97 adopts an alpha-helical coiled-coil tertiary structure and binds immunoglobulin and collagen. Nai\u0308ve mice infected with<jats:italic>S. japonicum<\/jats:italic>produce anti-rSj97 immunoglobulin G (IgG) antibodies as early as 4 weeks postinfection, while sera collected from<jats:italic>S. japonicum<\/jats:italic>-infected individuals contain anti-rSj97 IgE antibodies. Our method for pilot-scale production of recombinant full-length paramyosin will facilitate preclinical evaluation of paramyosin as a vaccine for schistosomiasis.<\/jats:p>","DOI":"10.1128\/iai.00409-08","type":"journal-article","created":{"date-parts":[[2008,4,22]],"date-time":"2008-04-22T02:42:26Z","timestamp":1208832146000},"page":"3164-3169","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":36,"title":["Pilot-Scale Production and Characterization of Paramyosin, a Vaccine Candidate for Schistosomiasis Japonica"],"prefix":"10.1128","volume":"76","author":[{"given":"Mario","family":"Jiz","sequence":"first","affiliation":[{"name":"Center for International Health Research"},{"name":"Pathobiology Graduate Program, Brown University, Providence, Rhode Island"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hai-Wei","family":"Wu","sequence":"additional","affiliation":[{"name":"Center for International Health Research"},{"name":"Department of Pathogen Biology, Nanjing Medical University, Nanjing, Jiangsu, People's Republic of China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rui","family":"Meng","sequence":"additional","affiliation":[{"name":"Department of Pathogen Biology, Nanjing Medical University, Nanjing, Jiangsu, People's Republic of China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sunthorn","family":"Pond-Tor","sequence":"additional","affiliation":[{"name":"Center for International Health Research"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mindy","family":"Reynolds","sequence":"additional","affiliation":[{"name":"Pathobiology Graduate Program, Brown University, Providence, Rhode Island"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jennifer F.","family":"Friedman","sequence":"additional","affiliation":[{"name":"Center for International Health Research"},{"name":"Department of Pediatrics"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Remigio","family":"Olveda","sequence":"additional","affiliation":[{"name":"Research Institute for Tropical Medicine, Alabang, Muntinlupa City, Metro Manila, Philippines"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luz","family":"Acosta","sequence":"additional","affiliation":[{"name":"Research Institute for Tropical Medicine, Alabang, Muntinlupa City, Metro Manila, Philippines"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jonathan D.","family":"Kurtis","sequence":"additional","affiliation":[{"name":"Center for International Health Research"},{"name":"Department of Pathology and Laboratory Medicine, Rhode Island Hospital"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.pt.2005.01.001"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0001-706X(02)00048-7"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0264-410X(97)00071-6"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/0035-9203(89)90334-9"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.71.11.6402-6410.2003"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0001-706X(02)00045-1"},{"key":"e_1_3_2_8_2","unstructured":"List of orphan products designations and approvals. 1991"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.parint.2005.02.004"},{"key":"e_1_3_2_10_2","first-page":"45","volume":"114","year":"1997","unstructured":"Gobert, G. 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