Self-assembly processing of virus-like particles

Yap Chuan (2009). Self-assembly processing of virus-like particles PhD Thesis, Aust Institute for Bioengineering & Nanotechnology, The University of Queensland.

       
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Author Yap Chuan
Thesis Title Self-assembly processing of virus-like particles
School, Centre or Institute Aust Institute for Bioengineering & Nanotechnology
Institution The University of Queensland
Publication date 2009-02
Thesis type PhD Thesis
Supervisor Prof. Anton Middelberg
Dr. Linda Lua
Total pages 170
Total colour pages 20
Total black and white pages 150
Subjects 06 Biological Sciences
Abstract/Summary Virus-like particles (VLPs) are elegant functional architectures formed by the self-assembly of viral structural proteins. VLPs have been developed as vaccines against hepatitis B and cervical cancer, and have recently been shown in animal studies to provide protection against both seasonal and avian influenza following intranasal administration. This new class of vaccines offers unprecedented immunoprotection, inherent safety, and a simple route of administration. To realize the full potential of VLP technology as an efficient and responsive vaccine platform, this project exploits the parallel advancements in recombinant technology, analytical techniques and colloidal science to facilitate the swift and economical delivery of candidate VLP vaccines from laboratory to clinical trials, and ultimately into commercial production. Three areas of VLP production are specifically targeted in this work, i.e., VLP subunit production, particle characterisation and assembly. The major research outcomes in this work are: (i) establishment of a simple and economical VLP subunit production method which eliminates inefficient and complicated purification procedures necessitated by the current in vivo production methods; (ii) development of a high-resolution and high-throughput analytical method for rapid and reliable quality control check of VLP products; and (iii) establishment of the foundation to predict optimal VLP self-assembly conditions through molecular thermodynamics. These research outcomes collectively enhance the quantitative knowledge base in VLP assembly and may ultimately enable the development of a mechanistic and descriptive modelling approach to optimize VLP production. From a fundamental perspective, this work introduces the first experimental technique to measure protein interactions of viral subunits undergoing rapid, irreversible assembly reaction. Such information, when correlated with molecular details and assembly conditions may provide unique insights into the molecular switches responsible for viral assembly, unveiling the fundamental mechanism underpinning viral self-assembly.
Keyword Virus-like Particles
Vaccine
self-assembly
second virial coefficient
Protein-protein Interactions
light scattering
Additional Notes 20, 34, 36, 39, 55, 59, 93, 99, 100, 102-106, 110, 114, 117, 138, 160, 163

 
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Created: Thu, 24 Sep 2009, 15:29:00 EST by Mr Yap Chuan on behalf of Library - Information Access Service