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Associate Professor Michael Landsberg
Associate Professor

Michael Landsberg

Email: 
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

64 works between 2001 and 2024

1 - 20 of 64 works

Featured

2022

Journal Article

Cyclic ADP ribose isomers: Production, chemical structures, and immune signaling

Manik, Mohammad K., Shi, Yun, Li, Sulin, Zaydman, Mark A., Damaraju, Neha, Eastman, Samuel, Smith, Thomas G., Gu, Weixi, Masic, Veronika, Mosaiab, Tamim, Weagley, James S., Hancock, Steven J., Vasquez, Eduardo, Hartley-Tassell, Lauren, Kargios, Nestoras, Maruta, Natsumi, Lim, Bryan Y. J., Burdett, Hayden, Landsberg, Michael J., Schembri, Mark A., Prokes, Ivan, Song, Lijiang, Grant, Murray, DiAntonio, Aaron, Nanson, Jeffrey D., Guo, Ming, Milbrandt, Jeffrey, Ve, Thomas and Kobe, Bostjan (2022). Cyclic ADP ribose isomers: Production, chemical structures, and immune signaling. Science, 377 (6614) eadc8969, 1-11. doi: 10.1126/science.adc8969

Cyclic ADP ribose isomers: Production, chemical structures, and immune signaling

Featured

2021

Journal Article

A broadly protective antibody that targets the flavivirus NS1 protein

Modhiran, Naphak, Song, Hao, Liu, Lidong, Bletchly, Cheryl, Brillault, Lou, Amarilla, Alberto A., Xu, Xiaoying, Qi, Jianxun, Chai, Yan, Cheung, Stacey T. M., Traves, Renee, Setoh, Yin Xiang, Bibby, Summa, Scott, Connor A. P., Freney, Morgan E., Newton, Natalee D., Khromykh, Alexander A., Chappell, Keith J., Muller, David A., Stacey, Katryn J., Landsberg, Michael J., Shi, Yi, Gao, George F., Young, Paul R. and Watterson, Daniel (2021). A broadly protective antibody that targets the flavivirus NS1 protein. Science, 371 (6525), 190-194. doi: 10.1126/science.abb9425

A broadly protective antibody that targets the flavivirus NS1 protein

2020

Journal Article

Structures of fungal and plant acetohydroxyacid synthases

Lonhienne, Thierry, Low, Yu Shang, Garcia, Mario D., Croll, Tristan, Gao, Yan, Wang, Quan, Brillault, Lou, Williams, Craig M., Fraser, James A., McGeary, Ross P., West, Nicholas P., Landsberg, Michael J., Rao, Zihe, Schenk, Gerhard and Guddat, Luke W. (2020). Structures of fungal and plant acetohydroxyacid synthases. Nature, 586 (7828), 317-321+. doi: 10.1038/s41586-020-2514-3

Structures of fungal and plant acetohydroxyacid synthases

Featured

2019

Journal Article

Cryo-EM structures of the pore-forming A subunit from the Yersinia entomophaga ABC toxin

Piper, Sarah J., Brillault, Lou, Rothnagel, Rosalba, Croll, Tristan I., Box, Joseph K., Chassagnon, Irene, Scherer, Sebastian, Goldie, Kenneth N, Jones, Sandra A, Schepers, Femke, Hartley-Tassell, Lauren, Ve, Thomas, Busby, Jason N, Dalziel, Julie E, Lott, J Shaun, Hankamer, Ben, Stahlberg, Henning, Hurst, Mark R H and Landsberg, Michael J (2019). Cryo-EM structures of the pore-forming A subunit from the Yersinia entomophaga ABC toxin. Nature Communications, 10 (1) 1952, 1952. doi: 10.1038/s41467-019-09890-8

Cryo-EM structures of the pore-forming A subunit from the Yersinia entomophaga ABC toxin

Featured

2013

Journal Article

The BC component of ABC toxins is an RHS-repeat-containing protein encapsulation device

Busby, Jason N., Panjikar, Santosh, Landsberg, Michael J., Hurst, Mark R. H. and Lott, J. Shaun (2013). The BC component of ABC toxins is an RHS-repeat-containing protein encapsulation device. Nature, 501 (7468), 547-550. doi: 10.1038/nature12465

The BC component of ABC toxins is an RHS-repeat-containing protein encapsulation device

Featured

2011

Journal Article

3D structure of the Yersinia entomophaga toxin complex and implications for insecticidal activity

Landsberg, Michael J., Jones, Sandra A., Rothnagel, Rosalba, Busby, Jason N., Marshall, Sean D. G., Simpson, Robert M., Lott, J. Shaun, Hankamer, Ben and Hurst, Mark R. H. (2011). 3D structure of the Yersinia entomophaga toxin complex and implications for insecticidal activity. Proceedings of the National Academy of Sciences of the United States of America, 108 (51), 20544-20549. doi: 10.1073/pnas.1111155108

3D structure of the Yersinia entomophaga toxin complex and implications for insecticidal activity

2024

Journal Article

Mutations in linker-2 of KLF1 impair expression of membrane transporters and cytoskeletal proteins causing hemolysis

Huang, Stephen, Reed, Casie, Ilsley, Melissa, Magor, Graham, Tallack, Michael, Landsberg, Michael, Mitchell, Helen, Gillinder, Kevin and Perkins, Andrew (2024). Mutations in linker-2 of KLF1 impair expression of membrane transporters and cytoskeletal proteins causing hemolysis. Nature Communications, 15 (1) 7019, 1-16. doi: 10.1038/s41467-024-50579-4

Mutations in linker-2 of KLF1 impair expression of membrane transporters and cytoskeletal proteins causing hemolysis

2024

Journal Article

The ABC toxin complex from Yersinia entomophaga can package three different cytotoxic components expressed from distinct genetic loci in an unfolded state: the structures of both shell and cargo

Busby, Jason N., Trevelyan, Sarah, Pegg, Cassandra L., Kerr, Edward D., Schulz, Benjamin L., Chassagnon, Irene, Landsberg, Michael J., Weston, Mitchell K., Hurst, Mark R. H. and Lott, J. Shaun (2024). The ABC toxin complex from Yersinia entomophaga can package three different cytotoxic components expressed from distinct genetic loci in an unfolded state: the structures of both shell and cargo. IUCrJ, 11 (3), 299-308. doi: 10.1107/s2052252524001969

The ABC toxin complex from Yersinia entomophaga can package three different cytotoxic components expressed from distinct genetic loci in an unfolded state: the structures of both shell and cargo

2023

Conference Publication

TLR4 TIR domain higher-order assemblies reveal the structural basis of adaptor recruitment in Toll-like receptor signaling pathways

Nanson, J. D., Muusse, T. W., Li, Y., Pan, M., Landsberg, M. J., Vajjhala, P. R., Ve, T., Stacey, K. J. and Kobe, B. (2023). TLR4 TIR domain higher-order assemblies reveal the structural basis of adaptor recruitment in Toll-like receptor signaling pathways. XXVI IUCr Congress, Melbourne, VIC Australia, 22-29 August 2023. Hoboken, NJ United States: Wiley-Blackwell. doi: 10.1107/s2053273323086631

TLR4 TIR domain higher-order assemblies reveal the structural basis of adaptor recruitment in Toll-like receptor signaling pathways

2023

Conference Publication

Structural basis of an anti-cancer biological warhead bound to its target CDCP1 for the diagnosis and treatment of epithelial cancers

Kwah, Kayden, Gu, Weixi, Arachchige, Kasun S. A., He, Yaowu, Landsberg, Michael, Kobe, Bostjan and Hooper, John (2023). Structural basis of an anti-cancer biological warhead bound to its target CDCP1 for the diagnosis and treatment of epithelial cancers. XXVI IUCr Congress, Melbourne, VIC Australia, 22-29 August 2023. Hoboken, NJ United States: Wiley-Blackwell. doi: 10.1107/s2053273323084449

Structural basis of an anti-cancer biological warhead bound to its target CDCP1 for the diagnosis and treatment of epithelial cancers

2023

Conference Publication

Structural basis for activation and inhibition of the pro-neurodegenerative NADase SARM1

Shi, Y., Nanson, J., Gu, W., Masic, V., Mosaiab, T., Landsberg, M., Kobe, B. and Ve, T. (2023). Structural basis for activation and inhibition of the pro-neurodegenerative NADase SARM1. XXVI IUCr Congress, Melbourne, VIC Australia, 22-29 August 2023. Hoboken, NJ United States: Wiley-Blackwell. doi: 10.1107/s2053273323087776

Structural basis for activation and inhibition of the pro-neurodegenerative NADase SARM1

2023

Journal Article

Structure and antigenicity of divergent Henipavirus fusion glycoproteins

Isaacs, Ariel, Low, Yu Shang, Macauslane, Kyle L., Seitanidou, Joy, Pegg, Cassandra L., Cheung, Stacey T. M., Liang, Benjamin, Scott, Connor A. P., Landsberg, Michael J., Schulz, Benjamin L., Chappell, Keith J., Modhiran, Naphak and Watterson, Daniel (2023). Structure and antigenicity of divergent Henipavirus fusion glycoproteins. Nature Communications, 14 (1) 3577, 1-10. doi: 10.1038/s41467-023-39278-8

Structure and antigenicity of divergent Henipavirus fusion glycoproteins

2023

Journal Article

Recent insights into mechanisms of cellular toxicity and cell recognition associated with the ABC family of pore-forming toxins

Aleksandrova, Nadezhda A., Roche, Solace G., Low, Yu Shang and Landsberg, Michael J. (2023). Recent insights into mechanisms of cellular toxicity and cell recognition associated with the ABC family of pore-forming toxins. Biochemical Society Transactions, 51 (3), 1235-1244. doi: 10.1042/bst20221409

Recent insights into mechanisms of cellular toxicity and cell recognition associated with the ABC family of pore-forming toxins

2023

Conference Publication

Molecular architecture of nucleosome remodeling and deacetylase sub-complexes by integrative structure determination

Arvindekar, Shreyas M., Jackman, Matthew J., Low, Jason K. K., Landsberg, Michael J., Mackay, Joel P. and Viswanath, Shruthi (2023). Molecular architecture of nucleosome remodeling and deacetylase sub-complexes by integrative structure determination. Biophysical Society 67th Annual Meeting, San Diego, CA, United States, 18-22 February 2023. St. Louis, MO, United States: Cell Press.

Molecular architecture of nucleosome remodeling and deacetylase sub-complexes by integrative structure determination

2023

Conference Publication

Molecular architecture of nucleosome remodeling and deacetylase sub-complexes by integrative structure determination

Arvindekar, Shreyas M., Jackman, Matthew J., Low, Jason K.K., Landsberg, Michael J., Mackay, Joel P. and Viswanath, Shruthi (2023). Molecular architecture of nucleosome remodeling and deacetylase sub-complexes by integrative structure determination. 67th Biophysical Society Annual Meeting 2023, San Diego, CA United States, 18-22 February 2023. St Louis, MO United States: Cell Press. doi: 10.1016/j.bpj.2022.11.2531

Molecular architecture of nucleosome remodeling and deacetylase sub-complexes by integrative structure determination

2022

Journal Article

Molecular architecture of nucleosome remodeling and deacetylase sub‐complexes by integrative structure determination

Arvindekar, Shreyas, Jackman, Matthew J., Low, Jason K. K., Landsberg, Michael J., Mackay, Joel P. and Viswanath, Shruthi (2022). Molecular architecture of nucleosome remodeling and deacetylase sub‐complexes by integrative structure determination. Protein Science, 31 (9) e4387, 1-19. doi: 10.1002/pro.4387

Molecular architecture of nucleosome remodeling and deacetylase sub‐complexes by integrative structure determination

2022

Conference Publication

Structural basis of TIR-domain assembly formation in TRAM- and TRIF- dependent TLR signalling

Pan, M., Hedger, A., Nanson, J., Pospich, S., Ve, T. V. E. A., Raunser, S., Landsberg, M. and Kobe, B. (2022). Structural basis of TIR-domain assembly formation in TRAM- and TRIF- dependent TLR signalling. 2022 American Crystallographic Association Meeting, Portland, OR USA, 29 July-3 August 2022. Hoboken, NJ USA: Wiley-Blackwell Publishing. doi: 10.1107/s2053273322093196

Structural basis of TIR-domain assembly formation in TRAM- and TRIF- dependent TLR signalling

2022

Journal Article

Enhancing the Thermal and Kinetic Stability of Ketol-Acid Reductoisomerase, a Central Catalyst of a Cell-Free Enzyme Cascade for the Manufacture of Platform Chemicals

Lv, You, Zheng, Shan, Goldenzweig, Adi, Liu, Fengjiang, Gao, Yan, Yang, Xiuna, Kandale, Ajit, McGeary, Ross P., Williams, Simon, Kobe, Bostjan, Schembri, Mark A., Landsberg, Michael J., Wu, Bin, Brück, Thomas B., Sieber, Volker, Boden, Mikael, Rao, Zihe, Fleishman, Sarel J., Schenk, Gerhard and Guddat, Luke W. (2022). Enhancing the Thermal and Kinetic Stability of Ketol-Acid Reductoisomerase, a Central Catalyst of a Cell-Free Enzyme Cascade for the Manufacture of Platform Chemicals. Applied Biosciences, 1 (2), 163-178. doi: 10.3390/applbiosci1020011

Enhancing the Thermal and Kinetic Stability of Ketol-Acid Reductoisomerase, a Central Catalyst of a Cell-Free Enzyme Cascade for the Manufacture of Platform Chemicals

2022

Journal Article

Structural basis of SARM1 activation, substrate recognition, and inhibition by small molecules

Shi, Yun, Kerry, Philip S., Nanson, Jeffrey D., Bosanac, Todd, Sasaki, Yo, Krauss, Raul, Saikot, Forhad K., Adams, Sarah E., Mosaiab, Tamim, Masic, Veronika, Mao, Xianrong, Rose, Faith, Vasquez, Eduardo, Furrer, Marieke, Cunnea, Katie, Brearley, Andrew, Gu, Weixi, Luo, Zhenyao, Brillault, Lou, Landsberg, Michael J., DiAntonio, Aaron, Kobe, Bostjan, Milbrandt, Jeffrey, Hughes, Robert O. and Ve, Thomas (2022). Structural basis of SARM1 activation, substrate recognition, and inhibition by small molecules. Molecular Cell, 82 (9), 1643-1659.e10. doi: 10.1016/j.molcel.2022.03.007

Structural basis of SARM1 activation, substrate recognition, and inhibition by small molecules

2022

Journal Article

Dermal delivery of a SARS-CoV-2 subunit vaccine induces immunogenicity against variants of concern

McMillan, Christopher L. D., Azuar, Armira, Choo, Jovin J. Y., Modhiran, Naphak, Amarilla, Alberto A., Isaacs, Ariel, Honeyman, Kate E., Cheung, Stacey T. M., Liang, Benjamin, Wurm, Maria J., Pino, Paco, Kint, Joeri, Fernando, Germain J. P., Landsberg, Michael J., Khromykh, Alexander A., Hobson-Peters, Jody, Watterson, Daniel, Young, Paul R. and Muller, David A. (2022). Dermal delivery of a SARS-CoV-2 subunit vaccine induces immunogenicity against variants of concern. Vaccines, 10 (4) 578, 578. doi: 10.3390/vaccines10040578

Dermal delivery of a SARS-CoV-2 subunit vaccine induces immunogenicity against variants of concern

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

    The structural basis of cell specificity in ABC toxins

    Principal Advisor

    Other advisors: Dr Evelyne Deplazes

  • 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

    Other advisors: Honorary Professor John Hooper

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

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