The Acinetobacter baumannii disinfectant resistance protein, AmvA, is a spermidine and spermine efflux pump

Francesca L. Short, Qi Liu, Bhumika Shah, Heather E. Clift, Varsha Naidu, Liping Li, Farzana T. Prity, Bridget C. Mabbutt, Karl A. Hassan, Ian T. Paulsen

Research output: Contribution to journalArticleResearchpeer-review

15 Citations (Scopus)

Abstract

Antimicrobial resistance genes, including multidrug efflux pumps, evolved long before the ubiquitous use of antimicrobials in medicine and infection control. Multidrug efflux pumps often transport metabolites, signals and host-derived molecules in addition to antibiotics or biocides. Understanding their ancestral physiological roles could inform the development of strategies to subvert their activity. In this study, we investigated the response of Acinetobacter baumannii to polyamines, a widespread, abundant class of amino acid-derived metabolites, which led us to identify long-chain polyamines as natural substrates of the disinfectant efflux pump AmvA. Loss of amvA dramatically reduced tolerance to long-chain polyamines, and these molecules induce expression of amvA through binding to its cognate regulator AmvR. A second clinically-important efflux pump, AdeABC, also contributed to polyamine tolerance. Our results suggest that the disinfectant resistance capability that allows A. baumannii to survive in hospitals may have evolutionary origins in the transport of polyamine metabolites.

Original languageEnglish
Article number1114
Number of pages12
JournalCommunications Biology
Volume4
Issue number1
DOIs
Publication statusPublished - Dec 2021

Cite this