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Title: Cell Surface Recognitions by Viral and Immune Receptors
Author: Yuan, Fang
ISNI:       0000 0001 3576 1545
Awarding Body: University of Oxford
Current Institution: University of Oxford
Date of Award: 2007
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Cell surface recognition is an important interaction occurring between proteins on opposite cell surfaces and transmits signals that allow cells to adapt to their environment. Viruses utilise recognition for entering host cells, and the immune system may defend against numerous attacks from environment through these interactions, by generating a protective adaptive immune response. This thesis offers insight into cell surface recognition through both viral and immune system molecules. For virus research, West Nile virus receptor binding domain was refolded and crystallized. Structural information ofthis domain was obtained and analysed. A putative receptor binding loop was identified from the structure. For immune research, T cell receptors that recognized Melan-A peptide, ELAGIGILTV, and gplOO peptide, YLEPGPVTV, were identified from several CD8+ T cell clones. Kinetic studies of these TCRs were carried out against rel<\ted human peptide-major histocompatibility complex by using surface plasmon resonance techniques. One ofthese TCRs which recognize Melan-A peptide was successfully crystallized with its ligand peptide-major histocompatibility complex. .J i Structural information obtained from X-ray diffraction studies ofviral and immune molecules indicated that protein-protein interactions are often effected by disordered/flexible regions in protein structures. For viruses, this flexible region is the binding loop and for T cell r.eceptors it is the complementarity determining regions. Such conformational flexibility allows specific protein interactions distinguishing small differences in amino acid composition. Alteration ofthe flexible regions of virus could be a potential mechanism to prevent cell entry and similarly, alteration of complementarity determining regions ofT cell receptors could lead to higher affmity for its ligand, major histocompatibility complex.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available