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Antimicrobial Synergy of a Ribonuclease and a Peptide Secreted by Human Cells
Name
nihms-1639445.pdf
Description
Accepted version
Size
1.05 MB
Format
Adobe PDF
Checksum (MD5)
0029426f3318e3a644aba9f5f4e49bd0
Author(s)
Eller, Chelcie H
Raines, Ronald T
Date Issued
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).
Terms of Use
Creative Commons Attribution-Noncommercial-Share Alike
Persistent DSpace Link
DOI of Published Version
10.1021/ACSINFECDIS.0C00594
