Journal article
Communication between viruses guides lysis-lysogeny decisions
Nature, Vol.541(7638), pp.488-493
26/Jan/2017
Abstract
Temperate viruses can become dormant in their host cells, a process called lysogeny. In every infection, such viruses decide between the lytic and the lysogenic cycles, that is, whether to replicate and lyse their host or to lysogenize and keep the host viable. Here we show that viruses (phages) of the SPbeta group use a small-molecule communication system to coordinate lysis-lysogeny decisions. During infection of its Bacillus host cell, the phage produces a six aminoacids-long communication peptide that is released into the medium. In subsequent infections, progeny phages measure the concentration of this peptide and lysogenize if the concentration is sufficiently high. We found that different phages encode different versions of the communication peptide, demonstrating a phage-specific peptide communication code for lysogeny decisions. We term this communication system the 'arbitrium' system, and further show that it is encoded by three phage genes: aimP, which produces the peptide; aimR, the intracellular peptide receptor; and aimX, a negative regulator of lysogeny. The arbitrium system enables a descendant phage to 'communicate' with its predecessors, that is, to estimate the amount of recent previous infections and hence decide whether to employ the lytic or lysogenic cycle.
Details
- Title
- Communication between viruses guides lysis-lysogeny decisions
- Creators
- Zohar Erez (null) - 972WIS_INST___111Ida Steinberger-Levy (null) - Israel Institute for Biological ResearchMaya Shamir (null) - Weizmann Institute of ScienceShany Doron (null) - 972WIS_INST___111Avihail, Avigail Stokar Avihail (null) - 972WIS_INST___111Yoav Peleg (null) - 972WIS_INST___f03Sarah Melamed (null) - Weizmann Institute of ScienceAzita Leavitt (null) - The Weizmann Institute of Science, Weizmann Institute of ScienceAlon Savidor (null) - 972WIS_INST___890Shira Albeck (null) - 972WIS_INST___f03Gil Amitai (Corresponding Author) - 972WIS_INST___111Rotem Sorek (Corresponding Author) - 972WIS_INST___111
- Resource Type
- Journal article
- Publication Details
- Nature, Vol.541(7638), pp.488-493; 26/Jan/2017
- Number of pages
- 6
- Language
- English
- DOI
- https://doi.org/10.1038/nature21049
- Grant note
- Israel Science Foundation [1303/12, 1360/16, 1796/12]; European Research Council (ERC) [ERC-StG 260432, ERC-CoG 681203]; Human Frontier Science Program (HFSP) [RGP0011/2013]; Abisch-Frenkel foundation; Pasteur-Weizmann council; Minerva Foundation; Leona M. and Harry B. Helmsley Charitable Trust; DFG; Dana and Yossie Holander Center for Structural Proteomics We thank J. Peters and C. Gross for sharing the Bacillus dCas9 system; A. Eldar for the oppD mutant and for advice on quorum sensing systems in Bacilli; I. Kolodkin-Gal for the 3610 strain; Y. Levin from the de Botton Institute for Protein Profiling for assistance in mass spectrometry; D. Fass and G. Armoni for advice regarding protein structure; and H. Sharir for assistance in the microscale thermophoresis analysis. We also thank D. Pollack, I. Kolodkin-Gal, O. Dym and T. Unger for support and discussion throughout the study. R.S. was supported, in part, by the Israel Science Foundation (personal grants 1303/12, 1360/16 and I-CORE grant 1796/12), the European Research Council (ERC) (grants ERC-StG 260432 and ERC-CoG 681203), Human Frontier Science Program (HFSP grant RGP0011/2013), the Abisch-Frenkel foundation, the Pasteur-Weizmann council grant, the Minerva Foundation, the Leona M. and Harry B. Helmsley Charitable Trust, and by a Deutsch-Israelische Projektkooperation (DIP) grant from the DFG. The ISPC is supported by the Dana and Yossie Holander Center for Structural Proteomics._ALMAME_DELIMITER_
- Record Identifier
- 993267193003596
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