Bacteriophage T5 tail tube structure suggests a trigger mechanism for Siphoviridae DNA ejection

Charles-Adrien Arnaud, Grégory Effantin, Corinne Vivès, Sylvain Engilberge, Maria Bacia, Pascale Boulanger, Eric Girard, Guy Schoehn and Cécile Breyton ()
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Charles-Adrien Arnaud: Université Grenoble Alpes, CNRS, CEA, Institut for Structural Biology (IBS)
Grégory Effantin: Université Grenoble Alpes, CNRS, CEA, Institut for Structural Biology (IBS)
Corinne Vivès: Université Grenoble Alpes, CNRS, CEA, Institut for Structural Biology (IBS)
Sylvain Engilberge: Université Grenoble Alpes, CNRS, CEA, Institut for Structural Biology (IBS)
Maria Bacia: Université Grenoble Alpes, CNRS, CEA, Institut for Structural Biology (IBS)
Pascale Boulanger: Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay
Eric Girard: Université Grenoble Alpes, CNRS, CEA, Institut for Structural Biology (IBS)
Guy Schoehn: Université Grenoble Alpes, CNRS, CEA, Institut for Structural Biology (IBS)
Cécile Breyton: Université Grenoble Alpes, CNRS, CEA, Institut for Structural Biology (IBS)

Nature Communications, 2017, vol. 8, issue 1, 1-9

Abstract: Abstract The vast majority of phages, bacterial viruses, possess a tail ensuring host recognition, cell wall perforation and safe viral DNA transfer from the capsid to the host cytoplasm. Long flexible tails are formed from the tail tube protein (TTP) polymerised as hexameric rings around and stacked along the tape measure protein (TMP). Here, we report the crystal structure of T5 TTP pb6 at 2.2 Å resolution. Pb6 is unusual in forming a trimeric ring, although structure analysis reveals homology with all classical TTPs and related tube proteins of bacterial puncturing devices (type VI secretion system and R-pyocin). Structures of T5 tail tubes before and after interaction with the host receptor were determined by cryo-electron microscopy at 6 Å resolution. Comparison of these two structures reveals that host-binding information is not propagated to the capsid through conformational changes in the tail tube, suggesting a role of the TMP in this information transduction process.

Date: 2017
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DOI: 10.1038/s41467-017-02049-3

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