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    • Research at UC

Dr Vanessa Kay Morris

Contact

Department: School of Biological Sciences

Email: vanessa.morris@canterbury.ac.nz

Direct Dial: +64 3 3690532

Office: Julius von Haast 422

Language: English

About
Research / Creative works
Supervision
Projects
Methods & Equipment

Fields of Research

  • Structural biology
  • Biophysics
  • Protein structure and interactions
  • Amyloid fibrils and protein aggregation
  • Protein misfolding diseases and neurodegeneration

Researcher Summary

My lab is focused on studying the structures, mechanisms and interactions of aggregating proteins. We are particularly interested in a certain fibre-like structure that is formed by a great variety of proteins called amyloid fibrils. We study amyloid proteins involved in disease, including Alzheimer's disease and motor neuron disease, as well as those that have functions in important biological processes.

The kinds of questions we are looking at include:
1) What are the functions of amyloids and aggregates in different biological processes?
2) What are the structural details of aggregates that have functional and disease-relevant roles?
3) How do other proteins and small molecules affect the aggregation of disease-relevant proteins, and at what stage do they affect aggregation? 4) What sequences are important for aggregation processes, and how can these be interfered with?
5) How do disease mutations affect aggregation or functional behaviour of aggregation-prone proteins?

We studying these topics with a range of structural and biophysical techniques including NMR spectroscopy (both solid-state and solution state), fluorescence-based aggregation assays, electron microscopy.

For more info, check out our webpage at www.morris-lab.com

Subject Area: Disciplines

  • Biology: Molecular, Cellular and Whole Organism Biology: Biochemistry; Biomolecular Interactions

Research/Scholarly/Creative Works

Journal Articles
  • Harper AR., Dobson RCJ., Morris VK. and Moggré GJ. (2022) Fermentation of plant-based dairy alternatives by lactic acid bacteria. Microbial Biotechnology 15(5): 1404-1421. http://dx.doi.org/10.1111/1751-7915.14008.
  • Smyth LCD., Murray HC., Hill M., van Leeuwen E., Highet B., Magon NJ., Osanlouy M., Mathiesen SN., Mockett B. and Singh-Bains MK. (2022) Neutrophil-vascular interactions drive myeloperoxidase accumulation in the brain in Alzheimer’s disease. Acta Neuropathologica Communications 10(1) http://dx.doi.org/10.1186/s40478-022-01347-2.
  • Göbl C., Morris VK., van Dam L., Visscher M., Polderman PE., Hartlmüller C., de Ruiter H., Hora M., Liesinger L. and Birner-Gruenberger R. (2020) Cysteine oxidation triggers amyloid fibril formation of the tumor suppressor p16INK4A. Redox Biology 28 http://dx.doi.org/10.1016/j.redox.2019.101316.
  • Brender JR., Ghosh A., Kotler SA., Krishnamoorthy J., Bera S., Morris V., Sil TB., Garai K., Reif B. and Bhunia A. (2019) Probing transient non-native states in amyloid beta fiber elongation by NMR. Chemical Communications 55(31): 4483-4486. http://dx.doi.org/10.1039/c9cc01067j.
  • Sun Y., Medina Cruz A., Hadley KC., Galant NJ., Law R., Vernon RM., Morris VK., Robertson J. and Chakrabartty A. (2019) Physiologically Important Electrolytes as Regulators of TDP-43 Aggregation and Droplet-Phase Behavior. Biochemistry 58(6): 590-607. http://dx.doi.org/10.1021/acs.biochem.8b00842.
  • Cristóvão JS., Morris VK., Cardoso I., Leal SS., Martínez J., Botelho HM., Göbl C., David R., Kierdorf K. and Alemi M. (2018) The neuronal S100B protein is a calcium-tuned suppressor of amyloid- aggregation. Science Advances 4(6) http://dx.doi.org/10.1126/sciadv.aaq1702.
  • Hora M., Carballo-Pacheco M., Weber B., Morris VK., Wittkopf A., Buchner J., Strodel B. and Reif B. (2017) Epigallocatechin-3-gallate preferentially induces aggregation of amyloidogenic immunoglobulin light chains. Scientific Reports 7: 41515-41515. http://dx.doi.org/10.1038/srep41515.
  • Hora M., Sarkar R., Morris V., Xue K., Prade E., Harding E., Buchner J. and Reif B. (2017) MAK33 antibody light chain amyloid fibrils are similar to oligomeric precursors. PLOS ONE 12(7) e0181799: 14. http://dx.doi.org/10.1371/journal.pone.0181799.
  • Linser R., Bardiaux B., Andreas LB., Hyberts SG., Morris VK., Pintacuda G., Sunde M., Kwan AH. and Wagner G. (2014) Solid-State NMR Structure Determination from Diagonal-Compensated, Sparsely Nonuniform-Sampled 4D Proton–Proton Restraints. Journal of the American Chemical Society 136(31): 11002-11010. http://dx.doi.org/10.1021/ja504603g.
  • Lo V., Ren Q., Pham C., Morris V., Kwan A. and Sunde M. (2014) Fungal Hydrophobin Proteins Produce Self-Assembling Protein Films with Diverse Structure and Chemical Stability. Nanomaterials 4(3): 827-843. http://dx.doi.org/10.3390/nano4030827.
  • Morris VK. and Sunde M. (2013) Formation of amphipathic amyloid monolayers from fungal hydrophobin proteins. Methods in Molecular Biology 996: 119-129. http://dx.doi.org/10.1007/978-1-62703-354-1_7.
  • Morris VK., Kwan AH. and Sunde M. (2013) Analysis of the Structure and Conformational States of DewA Gives Insight into the Assembly of the Fungal Hydrophobins. Journal of Molecular Biology 425(2): 244-256. http://dx.doi.org/10.1016/j.jmb.2012.10.021.
  • Yang W., Ren Q., Wu Y-N., Morris VK., Rey AA., Braet F., Kwan AH. and Sunde M. (2013) Surface functionalization of carbon nanomaterials by self-assembling hydrophobin proteins. Biopolymers 99(1): 84-94. http://dx.doi.org/10.1002/bip.22146.
  • Macindoe I., Kwan AH., Ren Q., Morris VK., Yang W., Mackay JP. and Sunde M. (2012) Self-assembly of functional, amphipathic amyloid monolayers by the fungal hydrophobin EAS. Proceedings of the National Academy of Sciences 109(14): E804-E811. http://dx.doi.org/10.1073/pnas.1114052109.
  • Morris VK., Kwan AH., Mackay JP. and Sunde M. (2012) Backbone and sidechain 1H, 13C and 15N chemical shift assignments of the hydrophobin DewA from Aspergillus nidulans. Biomolecular NMR Assignments 6(1): 83-86. http://dx.doi.org/10.1007/s12104-011-9330-5.
  • Morris VK., Linser R., Wilde KL., Duff AP., Sunde M. and Kwan AH. (2012) Solid-State NMR Spectroscopy of Functional Amyloid from a Fungal Hydrophobin: A Well-Ordered β-Sheet Core Amidst Structural Heterogeneity. Angewandte Chemie International Edition 51(50): 12621-12625. http://dx.doi.org/10.1002/anie.201205625.
  • Morris VK., Ren Q., Macindoe I., Kwan AH., Byrne N. and Sunde M. (2011) Recruitment of class I hydrophobins to the air:Water interface initiates a multi-step process of functional amyloid formation. Journal of Biological Chemistry 286(18): 15955-15963. http://dx.doi.org/10.1074/jbc.M110.214197.
  • Kwan AH., Macindoe I., Vukašin PV., Morris VK., Kass I., Gupte R., Mark AE., Templeton MD., Mackay JP. and Sunde M. (2008) The Cys3-Cys4 Loop of the Hydrophobin EAS Is Not Required for Rodlet Formation and Surface Activity. Journal of Molecular Biology 382(3): 708-720. http://dx.doi.org/10.1016/j.jmb.2008.07.034.
Chapters
  • Ball SR., Pham CLL., Lo V., Morris VK., Kwan AH. and Sunde M. (2020) Formation of Amphipathic Amyloid Monolayers from Fungal Hydrophobin Proteins. Methods in Molecular Biology: 55-72. http://dx.doi.org/10.1007/978-1-4939-9869-2_4.
  • Morris V. and Sunde M. (2013) Formation of amphipathic amyloid monolayers from fungal hydrophobin proteins.. In Gerrard JA (Ed.), Protein Nanotechnology - Protocols, Instrumentation, and Applications (Second Edition ed.): 119-129.Humana Press, Totowa, NJ. http://dx.doi.org/10.1007/978-1-62703-354-1.
Conference Contributions - Other
  • Morris V. (2019) A new role for the neuronal cytokine S100B: Suppression of amyloid-beta aggregation. Lorne, Australia: THE 44TH LORNE CONFERENCE ON PROTEIN STRUCTURE AND FUNCTION 2019, 10-14 Feb 2019.
  • Morris V. (2019) Cysteine oxidation triggers amyloid fibril formation by the tumour suppressor p16. Queenstown, New Zealand: Biomolecular Interactions and Engineering QMB Satellite Symposium, 1-2 Sep 2019.
  • Morris V. (2019) Polyphenol interactions with the Alzheimer’s disease peptide Aβ. Bunker Bay, Australia: The 12th Australian and New Zealand Society of Magnetic Resonance Conference, 25-28 Nov 2019.
  • Morris V. (2019) Redox-regulated amyloid fibril formation of the tumour suppressor p16. Singapore: 8th Asia-Pacific NMR Symposium 2019, 3-6 Jul 2019.
  • Morris V. (2018) S100B suppresses aggregation of the Alzheimer’s disease peptide amyloid-beta. Christchurch, New Zealand: BIC symposium 2018, 13-13 Dec 2018.
  • Morris V. (2016) Interaction of Alzheimer’s disease Amyloid-beta with the green-tea molecule EGCG. Kyoto, Japan: XXVIIth International Conference on Magnetic Resonance in Biological Systems (ICMRBS), 21-26 Aug 2016.
  • Morris V. (2015) Interaction of Alzheimer’s disease Amyloid beta with the green-tea molecule EGCG. Berlin, Germany: 3rd Workshop Structural Biology in the Helmholtz Association, 5-6 Nov 2015.
  • Morris V. (2015) Structural insights into EGCG-induced amyloid-beta oligomers. Prague, Czech Republic: European Congress on Magnetic Resonance (EUROMAR 2015), 5-11 Jul 2015.
  • Morris V. (2014) Solid-state NMR investigation of EGCG-induced Amyloid beta oligomers. Munich, Germany: North-Austrian/Bavarian Bio-NMR Workshop, 23 Oct 2014.
  • Morris V. (2014) Structural investigations of EGCG-induced Amyloid beta oligomers. Barcelona: Barcelona BioMed Conference. Amyloid-β and Alzheimer's Disease: From Fundamental Principles to Therapeutic Strategies, 9-11 Jul 2014.
  • Morris V. (2012) Insights into the structure and assembly process of a fibril-forming fungal protein. San Diego, U.S.A: 26th Annual Symposium of The Protein Society, 5-8 Aug 2012.
Theses / Dissertations
  • Morris V. (2013) Structural studies of the fibril-forming fungal hydrophobins. University of Sydney.

Student Supervision

Displaying all items.
    Current
  • PhD - Harper A: The role of lactic acid bacteria in fermentation of plant proteins for development of plant-based dairy alternatives
  • PhD - Heath S: Oxidation induced amyloid formation of the tumour suppressor protein p16
  • Masters - Ganderton J: Tears, alpha-synuclein and Parkinson’s disease
  • Honours - Schwartfeger A: Molecular Characterisation of the Aryl Hydrocarbon Receptor
  • Completed
  • Honours - Goldsmith D: Amyloid formation of human tumour suppressor protein p16 (2019)

Research Projects

  • Investigating molecular details of fibril formation by the crucial tumour suppressor p16
  • Unravelling molecular details of protein interactions that drive Alzheimers disease.

Key Methodologies

  • NMR spectroscopy
  • Electron microscopy
  • Protein aggregation assays
  • Protein expression and purification
  • Biophysical protein characterisation: FTIR, CD, SAXS, ITC
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