Tall tails: cryo-electron microscopy of phage tail DNA ejection conduits
- Author(s)
- Hardy, JM; Dunstan, RA; Lithgow, T; Coulibaly, F;
- Journal Title
- Biochemical Society Transactions
- Abstract
- The majority of phages, viruses that infect prokaryotes, inject their genomic material into their host through a tubular assembly known as a tail. Despite the genomic diversity of tailed phages, only three morphological archetypes have been described: contractile tails of Myoviridae-like phages; short non-contractile tails of Podoviridae-like phages; and long and flexible non-contractile tails of Siphoviridae-like phages. While early cryo-electron microscopy (cryo-EM) work elucidated the organisation of the syringe-like injection mechanism of contractile tails, the intrinsic flexibility of the long non-contractile tails prevented high-resolution structural determination. In 2020, four cryo-EM structures of Siphoviridae-like tail tubes were solved and revealed common themes and divergences. The central tube is structurally conserved and homologous to the hexameric rings of the tail tube protein (TTP) also found in contractile tails, bacterial pyocins, and type VI secretion systems. The interior surface of the tube presents analogous motifs of negatively charged amino acids proposed to facilitate ratcheting of the DNA during genome ejection. The lack of a conformational change upon genome ejection implicates the tape measure protein in triggering genome release. A distinctive feature of Siphoviridae-like tails is their flexibility. This results from loose inter-ring connections that can asymmetrically stretch on one side to allow bending and flexing of the tube without breaking. The outer surface of the tube differs greatly and may be smooth or rugged due to additional Ig-like domains in TTP. Some of these variable domains may contribute to adsorption of the phage to prokaryotic and eukaryotic cell surfaces affecting tropism and virulence.
- Publisher
- Portland Press
- Keywords
- bacteriophages; cryo-electron microscopy; protein structure; structural biology; virology
- Research Division(s)
- Chemical Biology
- Publisher's Version
- https://doi.org/10.1042/bst20210799
- Open Access at Publisher's Site
https://doi.org/10.1042/BST20210799- Terms of Use/Rights Notice
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Creation Date: 2022-02-18 10:38:02
Last Modified: 2022-02-18 11:09:37