Dr Andrew Gill

The Roslin Institute

Research Interests

Dr Gill’s core research focuses on defining how modifications to the primary and secondary structures of the prion protein contribute to prion protein function, prion protein structure and to the prion diseases that result when the prion protein misfolds. Dr Gill has defined specific structural motifs in the N-terminal region of the prion protein, a region previously thought to be unstructured, and contributed to the first crystal structure of recombinant prion protein. Recently, work has focussed on determining effects of polymorphisms of the prion gene on structural properties of the protein, based on assays to assess the propensity of protein to misfold. By assessing how cellular fractions aid the misfolding process, Dr Gill has identified subsets of molecules that potentially represent prion protein misfolding cofactors; one such cofactor is linked to prion protein function. Dr Gill is also interested in the normal function of the prion protein and in defining the repertoire of proteins whose expression levels depend on correct prion protein expression. A feature of Dr Gill's research is the application of diverse biochemical assays as well as multiple molecular dynamics simulations to understand protein structure. Dr Gill’s graduate training was in protein analysis by mass spectrometry, thereby initiating a long standing interest in the application of mass spectrometric and proteomic methods to the analysis of protein structure in general. As such, Dr Gill retains an interest in the application of mass spectrometric techniques to understand protein structure and interactions. More recently, Dr Gill has widened the use of mass spectrometric methods in biochemical analysis to encompass quantitation of specific metabolites in animal tissues.

Selected Publications

  • Mark Ritchie, Lawrence Hunt, Andy Gill. 2013. Lysine hydroxylation and O-glycosylation in the globular, C-terminal region of mammalian-expressed, recombinant PrP. International Journal of Mass Spectrometry Vol: 345 Pages: 132-141. More»
  • H Y Chen, A Gill, B K Dove, S R Emmett, C F Kemp, M A Ritchie, M Dee, J A Hiscox. 2005. Mass spectroscopic characterization of the coronavirus infectious bronchitis virus nucleoprotein and elucidation of the role of phosphorylation in RNA binding by using surface plasmon resonance. Journal of Virology Vol: 79 Pages: 1164-1179. More»
  • E W Blanch, A C Gill, A G O Rhie, J Hope, L Hecht, K Nielsen, L D Barron. 2004. Raman optical activity demonstrates poly(L-proline) II helix in the N-terminal region of the ovine prion protein: Implications for function and misfunction. Journal of Molecular Biology Vol: 343 Pages: 467-476. More»
  • L F Haire, S M Whyte, N Vasisht, A C Gill, C Verma, E J Dodson, G G Dodson, P M Bayley. 2004. The crystal structure of the globular domain of sheep prion protein. Journal of Molecular Biology Vol: 336 Pages: 1175-1183. More»
  • L H McColl, E W Blanch, A C Gill, A G O Rhie, M A Ritchie, L Hecht, K Nielsen, L D Barron. 2003. A new perspective on beta-sheet structures using vibrational Raman optical activity: From poly(L-lysine) to the prion protein. Journal of the American Chemical Society Vol: 125 Pages: 10019-10026. More»
  • Andy Gill, Mark A. Ritchie, Lawrence G. Hunt, Sarah E. Steane, Kenneth G. Davis, Sharon P. Bocking, Alexandre G. O. Rhie, Alan D. Bennett, James Hope. 2000. Post-translational hydroxylation at the N-terminus of the prion protein reveals presence of PPII structure in vivo. EMBO Journal Vol: 19 Pages: 5324-5331. More»
  • N. Sanghera, B. Correia, J.R.S. Correia, C. Ludwig, S. Agarwal, H.K. Nakamura, K. Kuwata, E. Samain, A.C. Gill, B.B. Bonev, T.J.T. Pinheiro. 2011. Deciphering the Molecular Details for the Binding of the Prion Protein to Main Ganglioside GM1 of Neuronal Membranes. Chemistry and Biology Vol: 18 Pages: 1422-1431. More»
  • J.F. Graham, D. Kurian, S. Agarwal, L. Toovey, L. Hunt, L. Kirby, T.J.T. Pinheiro, S.J. Banner, A.C. Gill. 2011. Na+/K+ -ATPase Is Present in Scrapie-Associated Fibrils, Modulates PrP Misfolding In Vitro and Links PrP Function and Dysfunction. PLoS One Vol: 6. More»
  • L. Kirby, S. Agarwal, J. F. Graham, W. Goldmann, A. C. Gill. 2010. Inverse correlation of thermal lability and conversion efficiency for five prion protein polymorphic variants. Biochemistry Vol: 49 Pages: 1448-59. More»
  • J. F. Graham, S. Agarwal, D. Kurian, L. Kirby, T. J. Pinheiro, A. C. Gill. 2010. Low Density Subcellular Fractions Enhance Disease-specific Prion Protein Misfolding. Journal of Biological Chemistry Vol: 285 Pages: 9868-9880. More»