The Structure of the Type III Secretion System Needle Complex
The type III secretion system (T3SS) is an essential virulence factor of many pathogenic bacterial species including Salmonella, Yersinia, Shigella and enteropathogenic Escherichia coli (EPEC). It is an intricate molecular machine that spans the bacterial
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Visualizing the Needle Complex ........................................................................................ A Structural Blueprint of the Needle Complex .................................................................. The Individual Building Blocks of the Needle Complex................................................... 3.1 The Inner Membrane Protein SctD ............................................................................ 3.2 The Second Inner Membrane Protein SctJ ................................................................ 3.3 The Outer Membrane Protein SctC ........................................................................... 3.4 The Needle Adaptor Protein SctI............................................................................... 3.5 The Needle Filament Protein SctF............................................................................. 3.6 The Tip Complex Protein SctA ................................................................................. 3.7 The Export Apparatus Proteins SctV, SctR, SctS, SctT and SctU ........................... 4 Assembly, Conformational Flexibility and Substrate Secretion......................................... 5 Future Directions ................................................................................................................. References ..................................................................................................................................
Abstract The type III secretion system (T3SS) is an essential virulence factor of many pathogenic bacterial species including Salmonella, Yersinia, Shigella and enteropathogenic Escherichia coli (EPEC). It is an intricate molecular machine that spans the bacterial membranes and injects effector proteins into target host cells, enabling bacterial infection. The T3SS needle complex comprises of proteinaceous rings supporting a needle filament which extends out into the extracellular environment. It serves as the central conduit for translocating effector proteins. Multiple laboratories have dedicated a remarkable effort to decipher the structure and function of the needle complex. A combination of structural biology techniques such as S. Miletic T. C. Marlovits (&) Center for Structural Systems Biology, Institute for Structural and Systems Biology, Universitätsklinikum Hamburg-Eppendorf, 85 Notkestraße, Hamburg 22607, Germany e-mail: [email protected] N. Goessweiner-Mohr Institute of Biophysics, Johannes Kepler University Linz, Gruberstraße 40, 4020 Linz, Austria e-mail: [email protected] Current Topics in Microbiology and Immunology https://doi.org/10.1007/82_2019_178 © Springer Nature Switzerland AG 2019
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cryo-electron microscopy (cryoEM), X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy and computer modelling have been utilized to study different structural components at progressively higher resolutions. This chapter will provide an overview of the structural details of th
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