Antimicrobial Synergy of a Ribonuclease and a Peptide Secreted by Human Cells
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nihms-1639445.pdf
Description
Accepted version
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1.05 MB
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Unknown
Checksum (MD5)
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Author(s)
Eller, Chelcie H.
Raines, Ronald T.
Date Issued
October 2020
Journal
ACS Infectious Diseases
Publisher
American Chemical Society (ACS)
Citation
Eller, Chelcie H and Raines, Ronald T. 2020. "Antimicrobial Synergy of a Ribonuclease and a Peptide Secreted by Human Cells." ACS Infectious Diseases, 6 (11).
Version
Author's final manuscript
Abstract
© LL-37 is a secretory peptide that has antimicrobial activity. Ribonuclease 1 (RNase 1) is a secretory enzyme that is not cytotoxic. We find that human LL-37 and human RNase 1 can act synergistically to kill Gram-negative bacterial cells. In the presence of nontoxic concentrations of LL-37, RNase 1 is toxic to Escherichia coli cells at picomolar levels. Using wild-type RNase 1 and an inactive variant labeled with a fluorophore, we observe the adherence of RNase 1 to E. coli cells and its cellular entry in the presence of LL-37. These data suggest a natural means of modulating the human microbiome via the cooperation of an endogenous peptide (37 residues) and small enzyme (128 residues).
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
Terms of Use
Creative Commons Attribution-Noncommercial-Share Alike
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DOI of Published Version
https://doi.org/10.1021/acsinfecdis.0c00594
