Kate Harvey is a current PhD candidate completing her thesis entitled “The characterisation of the cell surface of Staphylococcus aureus in the search for new therapeutic targets” within the ithree institute of the Science faculty at UTS. Her PhD project has allowed her to develop an expertise in the fields of molecular microbiology and microbial virulence, with a particular interest in the field of microbial proteomics. She has presented at international conferences, worked with collaborating laboratories in England and has been involved in a number of science communication and outreach programs (such as Pint of Science https://pintofscience.com.au/team/Sydney+Team).
Kate’s teaching experience includes teaching undergraduate students in the Faculty of Health and Faculty of Science as a casual academic at UTS since 2012. This role has included leading laboratory classes, leading tutorials, and facilitating student workshops. Further, she has had teaching roles as a mentor to students within the research laboratory including students completing undergraduate research programs, honours degrees, and international masters students. She is currently involved in a number of UTS grants aimed at improving student’s learning experiences with the implementation of Learning.Futures compliant course material in subjects such as Pathophysiology and Pharmacology 2 (91530) and Molecular Biology 1 (91132). In 2016 she received international recognition for her work in teaching, assessing, and giving feedback to learners being awarded as an Associate Fellow of the Higher Education Academy (AFHEA).
Molecular microbiology and microbial pathogenesis.
Coordinator for Pathophysiology and Pharmacology 2 (91530).
Currently a member of teaching staff for Pharmacology 1 (91707) and Molecular Biology 1 (91132).
Previously involved in Drug Discovery (91815), Pathophysiology and Pharmacology 3 (91527), Cell Biology and Genetics (91161), Health and Homeostasis (91528), General Microbiology (91314), and Proteomics (91536 - Masters by coursework),
Student mentor to a number of undergraduate research students, international masters students, and honours students.
Harvey, KL, Jarocki, VM, Charles, IG & Djordjevic, SP 2019, 'The Diverse Functional Roles of Elongation Factor Tu (EF-Tu) in Microbial Pathogenesis.', Frontiers in Microbiology, vol. 10.View/Download from: Publisher's site
Elongation factor thermal unstable Tu (EF-Tu) is a G protein that catalyzes the binding of aminoacyl-tRNA to the A-site of the ribosome inside living cells. Structural and biochemical studies have described the complex interactions needed to effect canonical function. However, EF-Tu has evolved the capacity to execute diverse functions on the extracellular surface of both eukaryote and prokaryote cells. EF-Tu can traffic to, and is retained on, cell surfaces where can interact with membrane receptors and with extracellular matrix on the surface of plant and animal cells. Our structural studies indicate that short linear motifs (SLiMs) in surface exposed, non-conserved regions of the molecule may play a key role in the moonlighting functions ascribed to this ancient, highly abundant protein. Here we explore the diverse moonlighting functions relating to pathogenesis of EF-Tu in bacteria and examine putative SLiMs on surface-exposed regions of the molecule.
Widjaja, M, Harvey, KL, Hagemann, L, Berry, IJ, Jarocki, V, Raymond, BBA, Tacchi, JL, Gründel, A, Steele, JR, Padula, MP, Charles, IG, Dumke, R & Djordjevic, SP 2017, 'Elongation factor Tu is a multifunctional and processed moonlighting protein.', Scientific Reports, vol. 7, no. 1, pp. 1-17.View/Download from: Publisher's site
Many bacterial moonlighting proteins were originally described in medically, agriculturally, and commercially important members of the low G + C Firmicutes. We show Elongation factor Tu (Ef-Tu) moonlights on the surface of the human pathogens Staphylococcus aureus (SaEf-Tu) and Mycoplasma pneumoniae (MpnEf-Tu), and the porcine pathogen Mycoplasma hyopneumoniae (MhpEf-Tu). Ef-Tu is also a target of multiple processing events on the cell surface and these were characterised using an N-terminomics pipeline. Recombinant MpnEf-Tu bound strongly to a diverse range of host molecules, and when bound to plasminogen, was able to convert plasminogen to plasmin in the presence of plasminogen activators. Fragments of Ef-Tu retain binding capabilities to host proteins. Bioinformatics and structural modelling studies indicate that the accumulation of positively charged amino acids in short linear motifs (SLiMs), and protein processing promote multifunctional behaviour. Codon bias engendered by an A + T rich genome may influence how positively-charged residues accumulate in SLiMs.