{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T01:55:43Z","timestamp":1760061343206,"version":"build-2065373602"},"reference-count":38,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2009,3,19]],"date-time":"2009-03-19T00:00:00Z","timestamp":1237420800000},"content-version":"vor","delay-in-days":18,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biotechnology Progress"],"published-print":{"date-parts":[[2009,3]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The development of hybridoma and recombinant DNA technologies has made it possible to use antibodies against cancer, autoimmune disorders, and infectious diseases in humans. These advances in therapy, as well as immunoprophylaxis, could also make it possible to use these technologies in agricultural species of economic importance such as pigs. Porcine reproductive and respiratory syndrome virus (PRRSV) is an arterivirus causing very important economic losses to the industry. Passive transfer of antibodies obtained by biotechnology could be used in the future to complement or replace vaccination against this and other pig pathogens. To this end, we constructed and studied the properties of chimeric mouse \u00d7 pig anti\u2010PRRSV antibodies. We cloned the constant regions of gamma\u20101 and gamma\u20102 heavy chains and the lambda light chain of pig antibodies in frame with the variable regions of heavy and light chains of mouse monoclonal antibody ISU25C1, which has neutralizing activity against PRRSV. The coding regions for chimeric IgG1 and IgG2 were expressed in a baculovirus expression system. Both chimeric antibodies recognized PRRSV in ELISA as well as in a Western\u2010blot format and, more importantly, were able to neutralize PRRSV in the same fashion as the parent mouse monoclonal antibody ISU25C1. In addition, we show that both pig IgG1 and IgG2 antibodies could bind complement component C1q, with IgG2 being more efficient than IgG1 in binding C1q. Expressing chimeric pig antibodies with protective capabilities offers a new alternative strategy for infectious disease control in domestic pigs. \u00a9 2009 American Institute of Chemical Engineers Biotechnol. Prog., 2009<\/jats:p>","DOI":"10.1002\/btpr.113","type":"journal-article","created":{"date-parts":[[2009,3,19]],"date-time":"2009-03-19T09:06:23Z","timestamp":1237453583000},"page":"516-523","source":"Crossref","is-referenced-by-count":4,"title":["Mouse \u00d7 pig chimeric antibodies expressed in Baculovirus retain the same properties of their parent antibodies"],"prefix":"10.1002","volume":"25","author":[{"given":"Ana M.","family":"Jar","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Fernando A.","family":"Osorio","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Osvaldo J.","family":"L\u00f3pez","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2009,3,19]]},"reference":[{"key":"e_1_2_6_2_2","doi-asserted-by":"publisher","DOI":"10.2460\/javma.2005.227.385"},{"key":"e_1_2_6_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.virol.2003.07.009"},{"key":"e_1_2_6_4_2","doi-asserted-by":"publisher","DOI":"10.1007\/s00705-007-0936-y"},{"key":"e_1_2_6_5_2","first-page":"176","article-title":"PRRSV: comparison of commercial vaccines in their ability to induce protection against current PRRSV strains of high virulence","volume":"25","author":"Osorio FA","year":"1998","journal-title":"Allen D Leman Swine Conf."},{"key":"e_1_2_6_6_2","doi-asserted-by":"publisher","DOI":"10.1099\/0022-1317-79-5-989"},{"key":"e_1_2_6_7_2","doi-asserted-by":"publisher","DOI":"10.1006\/viro.2002.1612"},{"key":"e_1_2_6_8_2","doi-asserted-by":"publisher","DOI":"10.1128\/CVI.00304-06"},{"key":"e_1_2_6_9_2","doi-asserted-by":"publisher","DOI":"10.1038\/289012a0"},{"key":"e_1_2_6_10_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.6623078"},{"key":"e_1_2_6_11_2","doi-asserted-by":"publisher","DOI":"10.1001\/jama.278.8.616"},{"key":"e_1_2_6_12_2","doi-asserted-by":"publisher","DOI":"10.1007\/978-3-540-73259-4_1"},{"key":"e_1_2_6_13_2","doi-asserted-by":"publisher","DOI":"10.1097\/00006454-199802000-00006"},{"key":"e_1_2_6_14_2","doi-asserted-by":"crossref","first-page":"3565","DOI":"10.4049\/jimmunol.153.8.3565","article-title":"Five putative subclasses of swine IgG identified from the cDNA sequences of a single animal","volume":"153","author":"Kacskovics Y","year":"1994","journal-title":"J Immunol."},{"key":"e_1_2_6_15_2","doi-asserted-by":"publisher","DOI":"10.1016\/0161-5890(91)90051-K"},{"volume-title":"Molecular Cloning. 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