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    Bacteriophage SPP1 tail tube protein self-assembles into β-structure rich tubes

    Langlois, C. and Ramboarina, S. and Cukkemane, A. and Auzat, I. and Chagot, B. and Gilquin, B. and Ignatiou, A. and Petitpas, I. and Kasotakis, E. and Paternostre, M. and White, H. E. and Orlova, Elena and Baldus, M. and Tavares, P. and Zinn-Justin, S. (2015) Bacteriophage SPP1 tail tube protein self-assembles into β-structure rich tubes. Journal of Biological Chemistry 390 , pp. 3836-3849. ISSN 0021-9258.

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    The majority of known bacteriophages have long tails that serve for bacterial target recognition and viral DNA delivery into the host. These structures form a tube from the viral capsid to the bacterial cell. The tube is formed primarily by a helical array of Tail Tube Protein (TTP) subunits. In phages with a contractile tail, the TTP tube is surrounded by a sheath structure. Here we report the first evidence that a phage TTP, gp17.1 of siphophage SPP1, self-assembles into long tubes in absence of other viral proteins. Gp17.1 does not exhibit a stable globular structure when monomeric in solution, even if it was confidently predicted to adopt the β-sandwich fold of phage λ TTP. However, Fourier Transform Infra-Red and Nuclear Magnetic Resonance spectroscopy analyses showed that its β-sheet content increases significantly during tube assembly, suggesting that gp17.1 acquires a stable β-sandwich fold only after self-assembly. EM analyses revealed that the tube is formed by hexameric rings stacked helicoidally with the same organization and helical parameters found for the tail of SPP1 virions. These parameters were used to build a pseudo-atomic model of the TTP tube. The large loop spanning residues 40-56 is located on the inner surface of the tube, at the interface between adjacent monomers and hexamers. In line with our structural predictions, deletion of this loop hinders gp17.1 tube assembly in vitro and interferes with SPP1 tail assembly during phage particle morphogenesis in bacteria.


    Item Type: Article
    Keyword(s) / Subject(s): bacteriophage, Fourier transform IR (FTIR), solid state NMR, tertiary structure, virus assembly, Electron Microscopy, Virion, tail tube
    School: Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences
    Research Centres and Institutes: Structural Molecular Biology, Institute of (ISMB)
    Depositing User: Administrator
    Date Deposited: 06 Jan 2015 09:38
    Last Modified: 02 Aug 2023 17:14


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