Postdoctoral Research Fellow
Overview
Qualifications
- Doctor of Philosophy, Charles Sturt University
Publications
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Journal Article: Structural characterization of a short-chain dehydrogenase/reductase from multi-drug resistant Acinetobacter baumannii
Cross, Emily M., Aragão, David, Smith, Kate M., Shaw, Karli I., Nanson, Jeffrey D., Raidal, Shane R. and Forwood, Jade K. (2019) Structural characterization of a short-chain dehydrogenase/reductase from multi-drug resistant Acinetobacter baumannii. Biochemical and Biophysical Research Communications, 518 3: 465-471. doi:10.1016/j.bbrc.2019.08.056
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Journal Article: NAD+ cleavage activity by animal and plant TIR domains in cell death pathways
Horsefield, Shane, Burdett, Hayden, Zhang, Xiaoxiao, Manik, Mohammad K., Shi, Yun, Chen, Jian, Qi, Tiancong, Gilley, Jonathan, Lai, Jhih-Siang, Rank, Maxwell X., Casey, Lachlan W., Gu, Weixi, Ericsson, Daniel J., Foley, Gabriel, Hughes, Robert O., Bosanac, Todd, von Itzstein, Mark, Rathjen, John P., Nanson, Jeffrey D., Boden, Mikael, Dry, Ian B., Williams, Simon J., Staskawicz, Brian J., Coleman, Michael P., Ve, Thomas, Dodds, Peter N. and Kobe, Bostjan (2019) NAD+ cleavage activity by animal and plant TIR domains in cell death pathways. Science, 365 6455: 793-799. doi:10.1126/science.aax1911
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Journal Article: Structural characterisation of β-Ketoacyl ACP synthase I bound to platencin and fragment screening molecules at two substrate binding sites
Patterson, Edward I., Nanson, Jeffrey D., Abendroth, Jan, Bryan, Cassie, Sankaran, Banumathi, Myler, Peter J. and Forwood, Jade K. (2019) Structural characterisation of β-Ketoacyl ACP synthase I bound to platencin and fragment screening molecules at two substrate binding sites. Proteins: Structure, Function, and Bioinformatics, . doi:10.1002/prot.25765
Available Projects
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Characterisation of higher-order assembly formation in Toll-like receptor (TLR) signaling pathways
Toll-like receptors (TLRs) detect pathogen- and endogenous danger-associated molecules (PAMPs/DAMPs) and initiate innate immune responses that lead to the production of pro-inflammatory cytokines. TLR signal transduction occurs through the cytoplasmic Toll/interleukin-1 receptor (TIR) domain of the receptor. Upon activation of TLRs, the TIR domain of the receptor recruits TIR-containing adaptor proteins. Recruitment of these adaptors via TIR domain:TIR domain interactions orchestrates downstream signaling pathways, leading to induction of the pro-inflammatory genes.
Recent efforts directed at elucidating the structural basis of TIR domain self-association suggest signaling by TLR and adaptor protein TIR domains occurs through a higher-order assembly mechanism termed signaling by co-operative assembly formation (SCAF) [1]. The TIR domain of adapter protein MAL has been shown to spontaneously form filaments (helical assemblies) in vitro, form assemblies with other TIR domains, and induce the formation of large MyD88 (myddosome-like) assemblies [2].
This project involves spectroscopy, electron microscopy, and crystallography to determine the structure of TLR signaling assemblies, and investigate the molecular mechanisms involved in the assembly formation and downstream signaling.
References [1] Nimma, S,. et al. (2017). “Towards the structure of the TIR-domain signalosome”. Current Opinion in Structural Biology, 43: 122-130. doi:10.1016/j.sbi.2016.12.014 [2] Ve, T,. et al. (2017). “Structural basis of TIR-domain-assembly formation in MAL- and MyD88-dependent TLR4 signaling”. Nature Structural and Molecular Biology, 24 9: 743-751. doi:10.1038/nsmb.3444
Publications
Journal Article
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Cross, Emily M., Aragão, David, Smith, Kate M., Shaw, Karli I., Nanson, Jeffrey D., Raidal, Shane R. and Forwood, Jade K. (2019) Structural characterization of a short-chain dehydrogenase/reductase from multi-drug resistant Acinetobacter baumannii. Biochemical and Biophysical Research Communications, 518 3: 465-471. doi:10.1016/j.bbrc.2019.08.056
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NAD+ cleavage activity by animal and plant TIR domains in cell death pathways
Horsefield, Shane, Burdett, Hayden, Zhang, Xiaoxiao, Manik, Mohammad K., Shi, Yun, Chen, Jian, Qi, Tiancong, Gilley, Jonathan, Lai, Jhih-Siang, Rank, Maxwell X., Casey, Lachlan W., Gu, Weixi, Ericsson, Daniel J., Foley, Gabriel, Hughes, Robert O., Bosanac, Todd, von Itzstein, Mark, Rathjen, John P., Nanson, Jeffrey D., Boden, Mikael, Dry, Ian B., Williams, Simon J., Staskawicz, Brian J., Coleman, Michael P., Ve, Thomas, Dodds, Peter N. and Kobe, Bostjan (2019) NAD+ cleavage activity by animal and plant TIR domains in cell death pathways. Science, 365 6455: 793-799. doi:10.1126/science.aax1911
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Patterson, Edward I., Nanson, Jeffrey D., Abendroth, Jan, Bryan, Cassie, Sankaran, Banumathi, Myler, Peter J. and Forwood, Jade K. (2019) Structural characterisation of β-Ketoacyl ACP synthase I bound to platencin and fragment screening molecules at two substrate binding sites. Proteins: Structure, Function, and Bioinformatics, . doi:10.1002/prot.25765
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Death, TIR, and RHIM: Self-assembling domains involved in innate immunity and cell-death signaling
Nanson, Jeffrey D., Kobe, Bostjan and Ve, Thomas (2019) Death, TIR, and RHIM: Self-assembling domains involved in innate immunity and cell-death signaling. Journal of Leukocyte Biology, 105 363-375. doi:10.1002/JLB.MR0318-123R
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Nanson, Jeffrey D., Rahaman, Habibur, Ve, Thomas and Kobe, Bostjan (2018) Regulation of signaling by cooperative assembly formation in mammalian innate immunity signalosomes by molecular mimics. Seminars in Cell and Developmental Biology, . doi:10.1016/j.semcdb.2018.05.002
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Soares Da Costa, Tatiana P., Nanson, Jeffrey D. and Forwood, Jade K. (2017) Structural characterisation of the fatty acid biosynthesis enzyme FabF from the pathogen Listeria monocytogenes. Scientific Reports, 7 1: 39277. doi:10.1038/srep39277
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Nanson, Jeffrey D. and Forwood, Jade K. (2015) Structural characterisation of FabG from yersinia pestis, a key component of bacterial fatty acid synthesis. PloS One, 10 11: . doi:10.1371/journal.pone.0141543
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Nanson, Jeffrey D., Himiari, Zainab, Swarbrick, Crystall M. D. and Forwood, Jade K. (2015) Structural characterisation of the Beta-Ketoacyl-Acyl carrier protein synthases, FabF and FabH, of Yersinia pestis. Scientific Reports, 5 . doi:10.1038/srep14797
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Swarbrick, Crystall M. D., Roman, Noelia, Cowieson, Nathan, Patterson, Edward I., Nanson, Jeffrey, Siponen, Marina I., Berglund, Helena, Lehtio, Lari and Forwood, Jade K. (2014) Structural basis for regulation of the human acetyl-CoA thioesterase 12 and interactions with the steroidogenic acute regulatory protein-related lipid transfer (START) domain. Journal of Biological Chemistry, 289 35: 24263-24274. doi:10.1074/jbc.M114.589408
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Crystallization and preliminary X-ray diffraction analysis of FabG from Yersinia pestis
Nanson, Jeffrey David and Forwood, Jade Kenneth (2014) Crystallization and preliminary X-ray diffraction analysis of FabG from Yersinia pestis. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 70 1: 101-104. doi:10.1107/S2053230X13033402
Possible Research Projects
Note for students: The possible research projects listed on this page may not be comprehensive or up to date. Always feel free to contact the staff for more information, and also with your own research ideas.
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Characterisation of higher-order assembly formation in Toll-like receptor (TLR) signaling pathways
Toll-like receptors (TLRs) detect pathogen- and endogenous danger-associated molecules (PAMPs/DAMPs) and initiate innate immune responses that lead to the production of pro-inflammatory cytokines. TLR signal transduction occurs through the cytoplasmic Toll/interleukin-1 receptor (TIR) domain of the receptor. Upon activation of TLRs, the TIR domain of the receptor recruits TIR-containing adaptor proteins. Recruitment of these adaptors via TIR domain:TIR domain interactions orchestrates downstream signaling pathways, leading to induction of the pro-inflammatory genes.
Recent efforts directed at elucidating the structural basis of TIR domain self-association suggest signaling by TLR and adaptor protein TIR domains occurs through a higher-order assembly mechanism termed signaling by co-operative assembly formation (SCAF) [1]. The TIR domain of adapter protein MAL has been shown to spontaneously form filaments (helical assemblies) in vitro, form assemblies with other TIR domains, and induce the formation of large MyD88 (myddosome-like) assemblies [2].
This project involves spectroscopy, electron microscopy, and crystallography to determine the structure of TLR signaling assemblies, and investigate the molecular mechanisms involved in the assembly formation and downstream signaling.
References [1] Nimma, S,. et al. (2017). “Towards the structure of the TIR-domain signalosome”. Current Opinion in Structural Biology, 43: 122-130. doi:10.1016/j.sbi.2016.12.014 [2] Ve, T,. et al. (2017). “Structural basis of TIR-domain-assembly formation in MAL- and MyD88-dependent TLR4 signaling”. Nature Structural and Molecular Biology, 24 9: 743-751. doi:10.1038/nsmb.3444
