Biochemical and Spectroscopic Observation of Mn(II) Sequestration from Bacterial Mn(II) Transport Machinery by Calprotectin
Name
nihms929713.pdf
Description
Accepted version
Size
1.45 MB
Format
Adobe PDF
Checksum (MD5)
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Author(s)
Hadley, Rose Currier
Brophy, Megan Brunjes
Gu, Yu
Nakashige, Toshiki George
Nolan, Elizabeth Marie
Date Issued
January 2018
Journal
Journal of the American Chemical Society
Publisher
American Chemical Society (ACS)
Citation
Hadley, Rose C. et al. “Biochemical and Spectroscopic Observation of Mn(II) Sequestration from Bacterial Mn(II) Transport Machinery by Calprotectin.” Journal of the American Chemical Society 140 (2018): 110-113 © 2018 The Author(s)
Version
Author's final manuscript
Abstract
Human calprotectin (CP, S100A8/S100A9 oligomer) is a metal-sequestering host-defense protein that prevents bacterial acquisition of Mn(II). In this work, we investigate Mn(II) competition between CP and two solute-binding proteins that Staphylococcus aureus and Streptococcus pneumoniae, Gram-positive bacterial pathogens of significant clinical concern, use to obtain Mn(II) when infecting a host. Biochemical and electron paramagnetic resonance (EPR) spectroscopic analyses demonstrate that CP outcompetes staphylococcal MntC and streptococcal PsaA for Mn(II). This behavior requires the presence of excess Ca(II) ions, which enhance the Mn(II) affinity of CP. This report presents new spectroscopic evaluation of two Mn(II) proteins important for bacterial pathogenesis, direct observation of Mn(II) sequestration from bacterial Mn(II) acquisition proteins by CP, and molecular insight into the extracellular battle for metal nutrients that occurs during infection.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
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Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.
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DOI of Published Version
https://doi.org/10.1021/JACS.7B11207
