Open AccessA hyperpromiscuous antitoxin protein domain for the neutralization of diverse toxin domains
Author(s) -
Tatsuaki Kurata,
Chayan Kumar Saha,
Jessica A. Buttress,
Toomas Mets,
Tetiana Brodiazhenko,
Kathryn Jane Turnbull,
Ololade F Awoyomi,
Sofia Raquel Alves Oliveira,
Steffi Jimmy,
Karin Ernits,
Maxence Delannoy,
Karina Persson,
Tanel Tenson,
Henrik Strahl,
Vasili Hauryliuk,
Gemma C. Atkinson
Publication year - 2022
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.2102212119
Subject(s) - antitoxin , biology , prophage , operon , plasmid , genetics , gene , lysogen , microbiology and biotechnology , computational biology , toxin , bacteriophage , escherichia coli
Significance Toxin–antitoxin systems are enigmatic and diverse elements of bacterial and bacteriophage genomes. We have uncovered remarkable versatility in an antitoxin protein domain that has evolved to neutralize dozens of different toxin domains. We find that antitoxins carrying this domain—Panacea—form complexes with their cognate toxins, indicating a direct neutralization mechanism, and that Panacea can be evolved to neutralize a noncognate and nonhomologous toxin with just two amino acid substitutions. This raises the possibility that this domain could be an adaptable universal or semi-universal protein neutralizer with significant biotechnological and medical potential.