{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,16]],"date-time":"2026-03-16T10:55:42Z","timestamp":1773658542085,"version":"3.50.1"},"reference-count":63,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2013,1,31]],"date-time":"2013-01-31T00:00:00Z","timestamp":1359590400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/3.0\/us\/"}],"content-domain":{"domain":["faseb.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FASEB Journal"],"published-print":{"date-parts":[[2013,5]]},"abstract":"<jats:p>\n                    Rabies kills many people throughout the developing world every year. The murine monoclonal antibody (mAb) 62\u201071\u20103 was recently identified for its potential application in rabies postexposure prophylaxis (PEP). The purpose here was to establish a plant\u2010based production system for a chimeric mouse\u2010human version of mAb 62\u201071\u20103, to characterize the recombinant antibody and investigate at a molecular level its interaction with rabies virus glycoprotein. Chimeric 62\u201071\u20103 was successfully expressed in\n                    <jats:italic>Nicotiana benthamiana.<\/jats:italic>\n                    Glycosylation was analyzed by mass spectroscopy; functionality was confirmed by antigen ELISA, as well as rabies and pseudotype virus neutralization. Epitope characterization was performed using pseudotype virus expressing mutagenized rabies glycoproteins. Purified mAb demonstrated potent viral neutralization at 500 IU\/mg. A critical role for antigenic site I of the glycoprotein, as well as for two specific amino acid residues (K226 and G229) within site I, was identified with regard to mAb 62\u201071\u20103 neutralization. Pseudotype viruses expressing glycoprotein from lyssaviruses known not to be neutralized by this antibody were the controls. The results provide the molecular rationale for developing 62\u201071\u20103 mAb for rabies PEP; they also establish the basis for developing an inexpensive plant\u2010based antibody product to benefit low\u2010income families in developing countries.\u2014Both, L., van Dolleweerd, C., Wright, E., Banyard, A. C., Bulmer\u2010Thomas, B., Selden, D., Altmann, F., Fooks, A. R., Ma, J. K.\u2010C. Production, characterization, and antigen specificity of recombinant 62\u201071\u20103, a candidate monoclonal antibody for rabies prophylaxis in humans.\n                    <jats:italic>FASEB J.<\/jats:italic>\n                    27, 2055\u20132065 (2013).\n                    <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.fasebj.org\">www.fasebj.org<\/jats:ext-link>\n                  <\/jats:p>","DOI":"10.1096\/fj.12-219964","type":"journal-article","created":{"date-parts":[[2013,2,1]],"date-time":"2013-02-01T08:29:49Z","timestamp":1359707389000},"page":"2055-2065","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":44,"title":["Production, characterization, and antigen specificity of recombinant 62\u201071\u20103, a candidate monoclonal antibody for rabies prophylaxis in humans"],"prefix":"10.1096","volume":"27","author":[{"given":"Leonard","family":"Both","sequence":"first","affiliation":[{"name":"Hotung Molecular Immunology Unit, Division of Clinical Sciences, St. George's University of London London UK"},{"name":"Animal Health and Veterinary Laboratories Agency Wildlife Zoonoses and Vector\u2010Borne Diseases Research Group, Department of Virology Weybridge UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Craig","family":"van Dolleweerd","sequence":"additional","affiliation":[{"name":"Hotung Molecular Immunology Unit, Division of Clinical Sciences, St. George's University of London London UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Edward","family":"Wright","sequence":"additional","affiliation":[{"name":"School of Life Sciences University of Westminster London UK"},{"name":"Wohl Virion Centre, Division of Infection and Immunity University College London London UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ashley C.","family":"Banyard","sequence":"additional","affiliation":[{"name":"Animal Health and Veterinary Laboratories Agency Wildlife Zoonoses and Vector\u2010Borne Diseases Research Group, Department of Virology Weybridge UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bianca","family":"Bulmer\u2010Thomas","sequence":"additional","affiliation":[{"name":"Wohl Virion Centre, Division of Infection and Immunity University College London London UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"David","family":"Selden","sequence":"additional","affiliation":[{"name":"Animal Health and Veterinary Laboratories Agency Wildlife Zoonoses and Vector\u2010Borne Diseases Research Group, Department of Virology Weybridge UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Friedrich","family":"Altmann","sequence":"additional","affiliation":[{"name":"Department of Chemistry University of Natural Resources and Life Sciences Vienna Austria"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Anthony R.","family":"Fooks","sequence":"additional","affiliation":[{"name":"Animal Health and Veterinary Laboratories Agency Wildlife Zoonoses and Vector\u2010Borne Diseases Research Group, Department of Virology Weybridge UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Julian K.\u2010C.","family":"Ma","sequence":"additional","affiliation":[{"name":"Hotung Molecular Immunology Unit, Division of Clinical Sciences, St. George's University of London London UK"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2013,1,31]]},"reference":[{"key":"e_1_2_7_2_1","first-page":"360","article-title":"Re\u2010evaluating the burden of rabies in Africa and Asia","volume":"83","author":"Knobel D. 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