2006 ASBMB Fellowship: Hilary Hoare

Hilary Hoare Hilary completed a BSc at Monash University in 2001, followed by an Honours year in the Department of Biochemistry and Molecular Biology, supervised by Professor David Jans, studying the nuclear transport of the dengue virus RNA-dependent RNA polymerase, NS5. Hilary then spent a year as a research assistant at the Australian Centre for Blood Diseases (Department of Medicine, Monash University), where she investigated the role of the GP-Ib-V-IX receptor in platelet adhesion and spreading.

In 2004, Hilary's interest in protein structure inspired her to begin a PhD under the supervision of Professor Jamie Rossjohn at the Protein Crystallography Unit at Monash. The focus of Hilary's PhD project has been an important immune receptor, HLA-E. HLA-E is a non-classical (1b) MHC molecule thought to function primarily as a ligand for the inhibitory NK cell receptor, NKG2A/CD94, to which it presents peptides derived from the leader sequences of other MHC-I molecules, thus acting as a checkpoint for classical MHC-I expression. However, a CMV-derived peptide, a mimic of classical class I leader peptides, can bind to HLA-E and generate an HLA-E-restricted T-cell response, suggesting a broader role for HLA-E in immunity. During her PhD, Hilary has investigated the role of HLA-E in the innate and adaptive immune response by using X-ray crystallography to structurally characterise its interactions with both NK cell receptors and an αβ T cell receptor (αβTCR). Last year she determined the crystal structure of an HLA-E-peptide complex bound to the αβTCR KK50.4. This work, published in Nature Immunology, is the first structure of an αβTCR/MHC-1b complex to be solved.

Hilary will use this ASBMB Fellowship to travel to Italy and attend the Como Crystallography School and the 38th Crystallographic Meeting in Erice, which will allow her an opportunity to learn more about crystallographic techniques and to present her recent findings in an international forum.

Previous Page | Top of Page
This page last modified: October 10, 2008.