Abstract
Tc (toxin complex) toxins are virulence factors of many insect- and human-pathogenic bacteria. They are composed of three subunits that act together to perforate the host membrane using a syringe-like injection mechanism. Thereby they translocate toxic enzymes into the cell, resulting ultimately in the death of the host cell. Our recent high-resolution structural and functional data explain the mechanism of action of this type of bacterial toxins in molecular detail.
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Roderer D, Raunser S (2019) Tc toxin complexes: assembly, membrane permeation, and protein translocation. Annu Rev Microbiol 73, doi: 10.1146/annurev-micro-102215-095531
Gatsogiannis C, Lang AE, Meusch D et al. (2013) A syringe-like injection mechanism in Photorhabdus luminescens toxins. Nature 495:520–523
Meusch D, Gatsogiannis C, Efremov RG et al. (2014) Mechanism of Tc toxin action revealed in molecular detail. Nature 508:61–65
Leidreiter F, Roderer D, Meusch D et al. (2019) Conserved architecture of Tc toxins from human and insect pathogenic bacteria. bioRxiv 596536, doi: 10.1101/596536
Piper SJ, Lou Brillault, Rothnagel R et al. (2019) Cryo-EM structures of the pore-forming A subunit from the Yersinia entomophaga ABC toxin. Nat Commun 10:1952
Gatsogiannis C, Merino F, Prumbaum D et al. (2016) Membrane insertion of a Tc toxin in near-atomic detail. Nat Struct Mol Biol 23:884–890
Lang AE, Schmidt G, Schlosser A et al. (2010) Photorhabdus luminescens toxins ADP-ribosylate actin and RhoA to force actin clustering. Science 327:1139–1142
Busby JN, Panjikar S, Landsberg MJ et al. (2013) The BC component of ABC toxins is an RHS-repeat-containing protein encapsulation device. Nature 501:547–550
Gatsogiannis C, Merino F, Roderer D et al. (2018) Tc toxin activation requires unfolding and refolding of a β-propeller. Nature 563:209–213
Roderer D, Hofnagel O, Benz R et al. (2019) Structure of a Tc holotoxin pore provides insights into the translocation mechanism. bioRxiv 7:590430, doi: 10.1101/590430
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Stefan Raunser 1995–2000 Biologie- und Chemiestudium, Universität Mainz. 2001–2004 Promotion, Max-Planck-Institut (MPI) für Biophysik. 2005–2008 Postdoc, Harvard Medical School, USA. 2008–2013 Emmy-Noether- Gruppenleiter, MPI für molekulare Physiologie. 2014 Einstein-Professor für Membranbiochemie, FU Berlin. Seit 2014 Direktor am MPI für molekulare Physiologie. Seit 2015 außerplanmäßiger Professor, TU Dortmund, und Honorarprofessor, Universität Duisburg-Essen.
Daniel Roderer 2004–2009 Biologiestudium an der Universität Regensburg. 2009–2014 Promotion an der ETH Zürich am Institut für Biophysik, danach bis 2015 Postdoc unter der Leitung von Prof. Dr. R. Glockshuber. Seit 2015 Postdoc am Max-Planck-Institut für molekulare Physiologie unter der Leitung von Prof. Dr. S. Raunser.
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Roderer, D., Raunser, S. Giftspritzen mit einzigartigem Injektionsmechanismus. Biospektrum 25, 500–503 (2019). https://doi.org/10.1007/s12268-019-1081-3
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DOI: https://doi.org/10.1007/s12268-019-1081-3