Contractile Tail Machines of Bacteriophages
Bacteriophages with contractile tails epitomize the concepts of “virus” and “phage” for many because the tails of these phages undergo a large conformational change – resembling the action of a syringe – upon the attachment to the host cell. The contractile tails belong to the recently recognized class of “contractile systems,” which includes phage tails, their close relatives R-type pyocins, the bacterial type VI secretion system, and the virulence cassette of Photorhabdus. Their function is to deliver large proteins and/or DNA into the cytoplasm of a bacterial or eukaryotic cell. The structure of the core components of all contractile tail-like systems is conserved, but the corresponding genes have diverged to such a degree that the common ancestry can no longer be easily detected at the level of amino acid sequence. At present, it is unclear, whether the contractile systems originated in bacteria or in phages. This chapter describes the structure and function of phage contractile tails and compares them with other phage tails and with other known contractile systems.
KeywordsTail Fiber T6SS Gene Gp18 Subunit Phage Tail Tape Measure Protein
We would like to express our sincere thank you to Prof. Michael Rossmann and Prof. Venigalla Rao, the editors of this book, for choosing the perfect timing in organizing this volume. This book was a unique opportunity for many scientists to summarize and publish the information, which was understood by many in the field because it was presented at conferences, but has never been published. We are very grateful to Prof. Rao for his great efforts in persuading the contributors to produce interesting chapters and, at the same time, keeping the entire project to a reasonable deadline.
Discussions with Prof. Alan Davidson, Prof. Ian Molineux, and Dr. Anastasia Aksyuk were extremely useful in preparation of this manuscript. We are very grateful to Prof. Liang Tong for sharing the coordinates of one of the sheath proteins prior to the publication of the paper describing the crystal structure.
- Coombs DH, Arisaka F (1994) T4 tail structure and function. In: Karam JD (ed) Molecular biology of bacteriophage T4. American Society for Microbiology, Washington, DC, pp 259–281Google Scholar
- Jacob F (1954) Biosynthèse induite et mode d’action d’une pyocin, antibiotique de Pseudomonas pyocyanea. Ann Inst Pasteur (Paris) 86:149–160Google Scholar
- Kuznetsova TA, Efimov AV, Aijrich LG, Kireeva IY, Marusich EI, Cappuccinelli P, Fiori P, Rappelli P, Kurochkina LP, Poglazov BF, Mesyanzhinov VV (1998) Properties of recombinant bacteriophage T4 tail sheath protein and its deletion fragments. Biochemistry (Mosc) 63:702–709Google Scholar
- Leiman PG, Battisti AJ, Bowman VD, Stummeyer K, Muhlenhoff M, Gerardy-Schahn R, Scholl D, Molineux IJ (2007) The structures of bacteriophages K1E and K1-5 explain processive degradation of polysaccharide capsules and evolution of new host specificities. J Mol Biol 371:836–849PubMedCrossRefGoogle Scholar