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Dr

Lou Brillault

Email: 
Phone: 
+61 7 344 36440

Overview

Background

My current role at UQ is cryoTEM scientist for the Centre for Microscopy and Microanalysis. I am in charge or monitoring UQ cryoTEM instruments as well as training and assisting UQ researchers that need to use this technique.

I completeed my PhD from UQ in 2018 where I studied the structure of the Vps4 oligomer using cryoEM under the supervisor of Prof. Michael Landsberg. During my PhD I have the opportunity to develop my skills at the University of Basel (Biozentrum) for a period of 6 months.

I have a deep experience on old and new generations of cryoTEM which helps me understanding the needs for the future of this tehcnique.

Availability

Dr Lou Brillault is:
Available for supervision

Qualifications

  • Bachelor of Science, Université d'Angers
  • Masters (Research), Université Claude Bernard Lyon 2
  • Doctor of Philosophy, The University of Queensland

Research interests

  • CryoEM

    I am interested in everything related to cryo-EM single-particle analysis. From developing new methodology to structural determination.

  • Program development related to cryoEM

    I have a particular interest in developing specific programs that facilitate acquiring and monitoring data for cryo-EM. The emergence of AI tools opens a new world where users do not need to interact with the intrusment anymore.

  • CryoEM methodology development

    I am passionate in studying the behaviour or protein complexes when trapped in vitreous ice. I enjoy studying and developing new methods to prevent these complexes to be degraded when interacting with the air-water interface. These methods can be simple like producing affinity grid with amourphous carbon or graphene oxide to something more complex like developing a new way to plunge freeze protein complexes.

  • Development of TEM facility management tools

    As a platform scientist my job is to make the life or our users easier for everyday use so they can focus on their research. I like to develop methodology using various computer programs to help them get their results as easyli and conveniently as possible. I also like to develop program tool that assist staff scientist when training or monitoring instruments of the facilty.

Research impacts

CryoEM is currently the major technique used to understand the structure of macromolecular complexes. To stay competitive in this field UQ researchers need highly-precise instrument and a good understanding of the technique. My role is to provide both by implementing easy and fast workflow as well as a solid training to cryoEM

Works

Search Professor Lou Brillault’s works on UQ eSpace

12 works between 2016 and 2026

1 - 12 of 12 works

Featured

2026

Journal Article

Molecular characterisation of the Bacillus subtilis SpbK antiphage defence system

Mishra, Biswa P., Loyo, Christian L., Cai, Yanyao, Litfin, Thomas, Miraj, Gause, Brillault, Lou, Masic, Veronika, Mosaiab, Tamim, Rajaratnam, Premraj, Rudrawar, Santosh, Gu, Weixi, Kobe, Bostjan, Gerdt, Joseph P., Grossman, Alan D., Shi, Yun and Ve, Thomas (2026). Molecular characterisation of the Bacillus subtilis SpbK antiphage defence system. Nature Communications, 17 (1) 1051, 1-16. doi: 10.1038/s41467-025-67810-5

Molecular characterisation of the Bacillus subtilis SpbK antiphage defence system

Featured

2025

Conference Publication

Structural and biochemical characterization of an antiphage defence system in Bacillus subtilis

Mishra, Biswa Prasanna, Masic, Veronika, Shi, Yun, Mosaiab, Tamim, Brillault, Lou and Ve, Thomas (2025). Structural and biochemical characterization of an antiphage defence system in Bacillus subtilis. 13th Asia Pacific Microscopy Congress, Brisbane, QLD Australia, 2-7 February 2025. Lexington, MA United States: ScienceOpen. doi: 10.14293/apmc13-2025-0221

Structural and biochemical characterization of an antiphage defence system in Bacillus subtilis

Featured

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

Featured

2021

Conference Publication

Structure, function and evolution of the orally active insecticidal toxin complex, YenTc

Piper, Sarah, Brillault, Lou, Box, Joseph, Low, Yu Shang, Chassagnon, Irene, Foley, Gabriel, Aleksandrova, Nadezhda, Hartley-Tassell, Lauren, Pegg, Cassandra, Schulz, Ben, Ve, Thomas, Lott, Shaun, Hurst, Mark and Landsberg, Michael (2021). Structure, function and evolution of the orally active insecticidal toxin complex, YenTc. XXV IUCr Congress, Prague, Czech Republic, 14-22 August 2021. International Union of Crystallography (IUCr). doi: 10.1107/s0108767321085950

Structure, function and evolution of the orally active insecticidal toxin complex, YenTc

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

Featured

2020

Journal Article

The nucleosome remodeling and deacetylase complex has an asymmetric, dynamic, and modular architecture

Low, Jason K. K., Silva, Ana P. G., Sharifi Tabar, Mehdi, Torrado, Mario, Webb, Sarah R., Parker, Benjamin L., Sana, Maryam, Smits, Callum, Schmidberger, Jason W., Brillault, Lou, Jackman, Matthew J., Williams, David C., Blobel, Gerd A., Hake, Sandra B., Shepherd, Nicholas E., Landsberg, Michael J. and Mackay, Joel P. (2020). The nucleosome remodeling and deacetylase complex has an asymmetric, dynamic, and modular architecture. Cell Reports, 33 (9) 108450, 108450. doi: 10.1016/j.celrep.2020.108450

The nucleosome remodeling and deacetylase complex has an asymmetric, dynamic, and modular architecture

Featured

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

2019

Book Chapter

Preparation of proteins and macromolecular assemblies for cryo-electron microscopy

Brillault, Lou and Landsberg, Michael J. (2019). Preparation of proteins and macromolecular assemblies for cryo-electron microscopy. Protein Nanotechnology: Protocols, Instrumentation, and Applications. (pp. 221-246) New York, NY, United States: Humana Press. doi: 10.1007/978-1-4939-9869-2_13

Preparation of proteins and macromolecular assemblies for cryo-electron microscopy

Featured

2018

Other Outputs

Structural characterisation of macromolecular complexes by cryo-electron microscopy

Brillault, Lou (2018). Structural characterisation of macromolecular complexes by cryo-electron microscopy. PhD Thesis, Institute for Molecular Bioscience, The University of Queensland. doi: 10.14264/09f636a

Structural characterisation of macromolecular complexes by cryo-electron microscopy

Featured

2017

Journal Article

Engineering recombinant virus-like nanoparticles from plants for cellular delivery

Brillault, Lou, Jutras, Philippe V., Dashti, Noor , Thuenemann, Eva C., Morgan, Garry, Lomonossoff, George P., Landsberg, Michael J. and Sainsbury, Frank (2017). Engineering recombinant virus-like nanoparticles from plants for cellular delivery. ACS Nano, 11 (4), 3476-3484. doi: 10.1021/acsnano.6b07747

Engineering recombinant virus-like nanoparticles from plants for cellular delivery

Featured

2016

Journal Article

The MTA1 subunit of the nucleosome remodeling and deacetylase complex can recruit two copies of RBBP4/7

Schmidberger, Jason W., Sharifi Tabar, Mehdi, Torrado, Mario, Silva, Ana P. G., Landsberg, Michael J., Brillault, Lou, AlQarni, Saad, Zeng, Yi Cheng, Parker, Benjamin L., Low, Jason K. K. and Mackay, Joel P. (2016). The MTA1 subunit of the nucleosome remodeling and deacetylase complex can recruit two copies of RBBP4/7. Protein Science, 25 (8), 1472-1482. doi: 10.1002/pro.2943

The MTA1 subunit of the nucleosome remodeling and deacetylase complex can recruit two copies of RBBP4/7

Funding

Past funding

  • 2015 - 2016
    Using SAXS to study nucleotide-dependent structural changes in a labile anti-viral drug target
    Australian Synchrotron Access Program
    Open grant

Supervision

Availability

Dr Lou Brillault is:
Available for supervision

Looking for a supervisor? Read our advice on how to choose a supervisor.

Supervision history

Completed supervision

Media

Enquiries

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communications@uq.edu.au