دورية
An E. colidisplay method for characterization of peptide–sensor kinase interactions
| العنوان: | An E. colidisplay method for characterization of peptide–sensor kinase interactions |
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| المؤلفون: | Brink, Kathryn R., Hunt, Maxwell G., Mu, Andrew M., Groszman, Ken, Hoang, Ky V., Lorch, Kevin P., Pogostin, Brett H., Gunn, John S., Tabor, Jeffrey J. |
| المصدر: | Nature Chemical Biology; 20220101, Issue: Preprints p1-9, 9p |
| مستخلص: | Bacteria use two-component system (TCS) signaling pathways to sense and respond to peptides involved in host defense, quorum sensing and inter-bacterial warfare. However, little is known about the broad peptide-sensing capabilities of TCSs. In this study, we developed an Escherichia colidisplay method to characterize the effects of human antimicrobial peptides (AMPs) on the pathogenesis-regulating TCS PhoPQ of SalmonellaTyphimurium with much higher throughput than previously possible. We found that PhoPQ senses AMPs with diverse sequences, structures and biological functions. We further combined thousands of displayed AMP variants with machine learning to identify peptide sub-domains and biophysical features linked to PhoPQ activation. Most of the newfound AMP activators induce PhoPQ in S. Typhimurium, suggesting possible roles in virulence regulation. Finally, we present evidence that PhoPQ peptide-sensing specificity has evolved across commensal and pathogenic bacteria. Our method enables new insights into the specificities, mechanisms and evolutionary dynamics of TCS-mediated peptide sensing in bacteria. |
| قاعدة البيانات: | Supplemental Index |
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Full Text Finder | تدمد: | 15524450 15524469 |
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| DOI: | 10.1038/s41589-022-01207-z |