Phage capsid recognition triggers activation of a bacterial toxin-antitoxin defense system

Leah M Smith; Peter C Fineran

doi:10.1016/j.molcel.2022.12.020

Phage capsid recognition triggers activation of a bacterial toxin-antitoxin defense system

Mol Cell. 2023 Jan 19;83(2):165-166. doi: 10.1016/j.molcel.2022.12.020.

Authors

Leah M Smith¹, Peter C Fineran²

Affiliations

¹ Department of Microbiology and Immunology, University of Otago, P.O. Box 56, Dunedin 9054, New Zealand; Genetics Otago, University of Otago, P.O. Box 56, Dunedin 9054, New Zealand.
² Department of Microbiology and Immunology, University of Otago, P.O. Box 56, Dunedin 9054, New Zealand; Genetics Otago, University of Otago, P.O. Box 56, Dunedin 9054, New Zealand; Bioprotection Aotearoa, University of Otago, P.O. Box 56, Dunedin 9054, New Zealand; Maurice Wilkins Centre for Molecular Biodiscovery, University of Otago, P.O. Box 56, Dunedin 9054, New Zealand. Electronic address: [email protected].

PMID: 36669478
DOI: 10.1016/j.molcel.2022.12.020

Abstract

Zhang et al.¹ reveal a previously unknown route to toxin activation whereby bacteriophage capsid proteins bind the antitoxin domain of the CapRel fused toxin-antitoxin system, triggering translational inhibition via pyrophosporylation of tRNAs and culminating in abortive infection-mediated phage resistance.

MeSH terms

Antitoxins* / metabolism
Bacteria / metabolism
Bacterial Proteins / metabolism
Bacterial Toxins* / genetics
Bacterial Toxins* / metabolism
Bacteriophages* / metabolism
Capsid / metabolism
Capsid Proteins / genetics
Toxin-Antitoxin Systems*

Substances

Capsid Proteins
Antitoxins
Bacterial Toxins
Bacterial Proteins