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Associate Professor Michael Landsberg
Associate Professor

Michael Landsberg

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Phone: 
+61 7 336 53756

Overview

Background

A/Prof Landsberg's undergraudate and Honours studies, majoring in Chemistry, were completed at Central Queensland University and the CSIRO (JM Rendel laboratories) before he moved to the University of Queensland to study a PhD in Biochemistry (awarded 2003). He then moved to a postdoctoral position at the Institute for Molecular Bioscience, spending time as a Visiting Scientist at Harvard Medical School (2008) and securing promotion to Senior Research Officer upon his return to IMB in 2009. He additioanlly spent time as a Visiting Scientist at the Victor Chang Cardiac Research Institute in 2010 and 2011.

In 2016, he joined UQ's School of Chemistry and Molecular Biosciences as a Group Leader in Cryo-EM and Macromolecular Structure and Senior Lecturer in Biochemistry and Biophysics, where he was promoted to Associate Professor in 2019. He has secured >$13.5M in competitive research funding since 2012, including major grants from the Australian Research Council and National Health and Medical Research Council. He his research has been presented at over 70 national and international conferences and research institutions.

Availability

Associate Professor Michael Landsberg is:
Available for supervision
Media expert

Qualifications

  • Doctor of Philosophy, The University of Queensland

Research interests

  • Single particle electron cryo-microscopy (cryo-EM) of molecular machines

    Structural biology has been largely founded on techniques developed and refined over the past 60+ years that involve measuring X-ray diffraction from protein crystals and relating to this to chemical structure. But structural biology is currently in the midst of a revolutionised, catalysed by recent advances in electron cryo-microscopy (cryo-EM) which now allow protein and macromolecular structures to be studied in near-atomic detail, without the need to first obtain protein crystals. Freed from the challenging pre-requisite to first obtain protein crystals, this recent development has paved the way for structural characterisation of a number of classes of challenging macromolecules, including membrane proteins, and multi-component protein and nucleic acid complexes. In our lab, we primarily employ cryo-EM as tool to study macromolecular structures from both of these groups.

  • Molecular mechanisms of microbial pathogenesis

    We have a particular interest in understanding fundamental mechanisms that enable infection by viruses and pathogenic bacteria, and that contribute to virulence associated with these infectious processes. Using cryo-EM, we study the structure in near-atomic details of molecules that are important in these processes. Examples include bacterial toxins belonging to A5BC class of pore-forming toxins and enveloped viruses (e.g. HIV, Ebola) that are dependent on the ESCRT machinery.

Research impacts

The arrival of the 'genomic era' at the start of the 21st century brought with it unprecedented capabilities to identify the genes and proteins that are linked to human diseases. But in the current, post-genomic era, it has become increasingly clear that a list of genes involved in disease is not enough. Genes and the proteins they encode rarely act in isolation; rather they form networks of interactions with proteins and other molecules. In order to understand how proteins maintain normal cellular function, how disfunctional proteins contribute to illness and disease, and to harness the potential of proteins to be used and targeted for health and biotechnological advancement, it is critical that we obtain a full appreciation of how proteins come together and interact, and how this translates to specifc functional consequences.

Dr Landsberg's research reflects a particular interest in a number of biological phenomena that are the result of proteins and other molecules coming together to function as multi-component molecular machineries. Together with colleagues, he discovered how a new family of bacterial pore-forming protein toxins are assembled into a multi-functional protein machinery that combines maturation, folding, transportation, targeting and injection of a potent cytotoxin into susceptible cells. These toxins were originally discovered in bateria that are naturally-occuring pathogens of insects and our discoveries have helped to guide strategies which might prove useful in the development of new biopesticides based on pore-forming toxins. His research interests also include manipulating the function of these proteins for other biotechnological applications that benefit from the targeted delivery of proteins and peptides to cells. Dr Landsberg also seeks to understand the role of multi-component protein machineries in endosomal protein trafficking, virus infection, immune signalling, the maintenance of genomic DNA structure, nucleoside biosynthesis and the movement of ions and small molecules across cellular membranes as facilitated by ion channel proteins. An improved understanding of these processes has the potential to do deliver impacts for the treatment of infectious diseases associated with pathogenic bacteria and viruses (e.g. HIV/AIDS, Ebola, Dengue and Zika viruses); various cancers; diseases of inflammation and immunity (e.g. arthrititis and auto-immune diseases) and the prevention of ischaemia following stroke.

Works

Search Professor Michael Landsberg’s works on UQ eSpace

65 works between 2001 and 2024

61 - 65 of 65 works

2006

Conference Publication

The role of alternative splicing and post-translational modifications of hnRNP A/B proteins and their subcellular localization

Landsberg, M.J., Hatfield, J.T., Friend, L., Dunphy, J., Cowan, D.W., Maggipinto, M. and Smith, R. W. (2006). The role of alternative splicing and post-translational modifications of hnRNP A/B proteins and their subcellular localization. ComBio 2006, Brisbane, Australia, 25-28 Sept, 2006. Kent Town, Australia: Australian Society for Biochemistry and Molecular Biology.

The role of alternative splicing and post-translational modifications of hnRNP A/B proteins and their subcellular localization

2006

Journal Article

A method for screening the temperature dependence of three-dimensional crystal formation

Landsberg, M. J., Bond, J., Gee, C. L., Martin, J. L. and Hankamer, B. (2006). A method for screening the temperature dependence of three-dimensional crystal formation. Acta Crystallographica Section D: Biological Crystallography, 62 (Pt 5), 559-562. doi: 10.1107/s0907444906006093

A method for screening the temperature dependence of three-dimensional crystal formation

2003

Other Outputs

Structural studies on the cytoplasmic RNA transport factor, hnRNP A2

Landsberg, Michael (2003). Structural studies on the cytoplasmic RNA transport factor, hnRNP A2. PhD Thesis, School of Molecular and Microbial Sciences, The University of Queensland. doi: 10.14264/106579

Structural studies on the cytoplasmic RNA transport factor, hnRNP A2

2002

Conference Publication

HnRNP A2 - a multifunctional nucleic acid-binding protein

Landsberg, M. J. and Smith, R. W. (2002). HnRNP A2 - a multifunctional nucleic acid-binding protein. ComBio 2002, Sydney, 29 September - 3 October, 2002.

HnRNP A2 - a multifunctional nucleic acid-binding protein

2001

Conference Publication

Structural analysis of the hnRNP A proteins: Understanding the interaction between hnRNP A2 and the A2RE trafficking element

Landsberg, M., Guddat, L. W., Hawkins, B. L. and Smith, R. W. (2001). Structural analysis of the hnRNP A proteins: Understanding the interaction between hnRNP A2 and the A2RE trafficking element. ASBMB, Canberra, 31 Sept-4 Oct, 2001.

Structural analysis of the hnRNP A proteins: Understanding the interaction between hnRNP A2 and the A2RE trafficking element

Funding

Current funding

  • 2022 - 2025
    The mechanistic basis of tropism in an insecticidal pore-forming toxin
    ARC Discovery Projects
    Open grant

Past funding

  • 2020 - 2021
    New generation direct electron detector for cryo-electron microscopy (ARC LIEF project administered by Monash University)
    Monash University
    Open grant
  • 2019 - 2022
    Structural insights into the function and antigenicity of the flavivirus NS1 protein
    NHMRC Project Grant
    Open grant
  • 2018 - 2019
    Automated high resolution & high contrast cryoTEM for 3D structural biology
    ARC Linkage Infrastructure, Equipment and Facilities
    Open grant
  • 2018
    Cryoelectron Microscopy Platform for Cellular Structural Biology
    UQ Major Equipment and Infrastructure
    Open grant
  • 2017 - 2021
    Structure and function of a cancer-linked co-regulator complex (NHMRC Project Grant administered by the University of Sydney)
    University of Sydney
    Open grant
  • 2017 - 2022
    Unveiling the molecular mechanism of bacterial ABC toxins
    ARC Discovery Projects
    Open grant
  • 2015 - 2016
    Using SAXS to study nucleotide-dependent structural changes in a labile anti-viral drug target
    Australian Synchrotron Access Program
    Open grant
  • 2015 - 2019
    RHS-repeat-containing proteins, a new paradigm for targeted protein delivery
    University of Auckland
    Open grant
  • 2015
    Combining gradient crosslinking and SAXS to stabilise and study nucleotide dependant structural changes in labile anti-drug target
    Australian Synchrotron Access Program
    Open grant
  • 2015 - 2016
    Reaching new heights in high-resolution electron microscopy
    ARC Linkage Infrastructure, Equipment and Facilities
    Open grant
  • 2015
    Protein Analysis Facility
    UQ Major Equipment and Infrastructure
    Open grant
  • 2013 - 2016
    Endosomal protein trafficking complexes - therapeutic targets for novel antivirals
    NHMRC Project Grant
    Open grant
  • 2008
    UQ Travel Awards Category 2 - Michael Landsberg
    UQ Travel Grants Scheme
    Open grant

Supervision

Availability

Associate Professor Michael Landsberg is:
Available for supervision

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Supervision history

Current supervision

  • Doctor Philosophy

    Structural Characterisation of the Nucleosome Remodelling and Deacetylase (NuRD) Complex

    Principal Advisor

    Other advisors: Dr Lou Brillault

  • Doctor Philosophy

    Using advanced imaging technologies to study cellular recognition by bacterial toxins

    Principal Advisor

    Other advisors: Dr Evelyne Deplazes

  • Doctor Philosophy

    Structure and Function of ScCAD, the first step of Pyrimidine Synthesis in Saccharomyces cerevisiae

    Principal Advisor

    Other advisors: Professor Benjamin Schulz, Professor Bostjan Kobe

  • Doctor Philosophy

    Structural and functional determinants of host specificity in ABC toxins

    Principal Advisor

    Other advisors: Dr Samantha Stehbens

  • Doctor Philosophy

    The structural basis of cell specificity in ABC toxins

    Principal Advisor

    Other advisors: Dr Evelyne Deplazes

  • Doctor Philosophy

    Characterisation of cellular receptors and membrane binding mechanisms utilized by YenTc

    Principal Advisor

    Other advisors: Professor Benjamin Schulz

  • Doctor Philosophy

    Investigating the molecular mechanism of cellular recognition by bacterial ABC toxins.

    Principal Advisor

    Other advisors: Dr Samantha Stehbens

  • Doctor Philosophy

    Molecular and cellular determinants of CDCP1 targeted, payload-delivery antibodies.

    Associate Advisor

  • Doctor Philosophy

    Proteins in innate immunity pathways: from protein structure to therapeutic targeting

    Associate Advisor

    Other advisors: Professor James Fraser, Professor Bostjan Kobe

Completed supervision

Media

Enquiries

Contact Associate Professor Michael Landsberg directly for media enquiries about:

  • antivirals
  • biopesticides
  • cryo-EM
  • CryoEM
  • electron microscopy
  • HIV
  • infectious disease
  • molecular microbiology
  • structural biology

Need help?

For help with finding experts, story ideas and media enquiries, contact our Media team:

communications@uq.edu.au