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Title: Structural and functional analysis of zona pellucida
Author: Koothan, Thillai
Awarding Body: University of Edinburgh
Current Institution: University of Edinburgh
Date of Award: 1994
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The ability of the zona pellucida to mediate the species specific recognition of spermatozoa is due to a glycoprotein constituent of this structure, known as ZP3. In view of its important role in the initiation of fertilization, ZP3 has been identified as a suitable candidate for the development of a contraceptive vaccine. In order to generate recombinant marmoset ZP3 for immunization purposes a full length 1.3 kb insert encoding for marmoset ZP3 was cloned downstream of the malE gene to generate a fusion protein containing marZP3 and a maltose binding domain. This protein was found to be generated in a soluble form in aqueous solutions and the antigenic integrity of this molecule was demonstrated by it capacity to be recognized by a monoclonal antibody raised against human ZP3. This full length fusion protein has been purified by anion exchange chromatography and used to generate polyclonal antibodies. In addition to these in vitro studies on the generation of a recombinant marZP3 for active immunization purposes, in vivo studies have also been performed on the induction of active immunity against porcine ZP3. These studies have demonstrated that an important side effect of induction of immunity against a heterologous ZP3 antigen involves the depletion of the primordial follicle pool. Moreover this pathology could be transferred to non-immunized recipients by the passive transfer of antibody. These data raise the important question as to whether a similar pathology would be induced if homologous zona antigens were used for the induction of immunity. As a result of the work descriebd in this thesis, this question can now be addressed in the marmoset monkey using recombinant marZP3 as antigen.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available