In order to characterize the protein product of the major capsid protein gene of Bovine Papillomavirus Type 2, 93% of the L1 open reading frame was cloned into two different expression vectors. This coding sequence produced a hybrid product when cloned into the expression vector pKK233-2, which interacted weakly with anti-BPV antisera and proved unable to elicit neutralizing antibodies. When the sequence was cloned into the expression vector pRA10, a more native form of the major capsid protein was produced, which interacted well with anti-BPV sera. Antisera raised against this cloned product was able to neutralize BPV in a tissue culture transformation assay. The 3' end of the L1 open reading frame was cloned into pBA10 in order to characterize the immunogenic potential of the carboxy terminus of the major capsid gene. The carboxy terminus proved to have no greater ability to interact with anti-BPV antisera, showing that the immunogenic epitopes of the protein are probably evenly distributed along the linear sequence.
| Identifer | oai:union.ndltd.org:arizona.edu/oai:arizona.openrepository.com:10150/184475 |
| Date | January 1988 |
| Creators | Driscoll, Barbara. |
| Publisher | The University of Arizona. |
| Source Sets | University of Arizona |
| Language | English |
| Detected Language | English |
| Type | text, Dissertation-Reproduction (electronic) |
| Rights | Copyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author. |
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