| Literature DB >> 6272395 |
D G Kleid, D Yansura, B Small, D Dowbenko, D M Moore, M J Grubman, P D McKercher, D O Morgan, B H Robertson, H L Bachrach.
Abstract
A DNA sequence coding for the immunogenic capsid protein VP3 of foot-and-mouth disease virus A12, prepared from the virion RNA, was ligated to a plasmid designed to express a chimeric protein from the Escherichia coli tryptophan promoter-operator system. When Escherichia coli transformed with this plasmid was grown in tryptophan-depleted media, approximately 17 percent of the total cellular protein was found to be an insoluble and stable chimeric protein. The purified chimeric protein competed equally on a molar basis with VP3 for specific antibodies to foot-and-mouth disease virus. When inoculated into six cattle and two swine, this protein elicited high levels of neutralizing antibody and protection against challenge with foot-and-mouth disease virus.Entities:
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Year: 1981 PMID: 6272395 DOI: 10.1126/science.6272395
Source DB: PubMed Journal: Science ISSN: 0036-8075 Impact factor: 47.728