Biochemical and Spectroscopic Observation of Mn(II) Sequestration from Bacterial Mn(II) Transport Machinery by Calprotectin
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-positiv...
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| Format: | Article |
| Language: | English |
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American Chemical Society (ACS)
2020
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| Online Access: | https://hdl.handle.net/1721.1/125599 |
| _version_ | 1826205133322584064 |
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| author | Hadley, Rose Currier Brophy, Megan Brunjes Gu, Yu Nakashige, Toshiki George Nolan, Elizabeth Marie |
| author2 | Massachusetts Institute of Technology. Department of Chemistry |
| author_facet | Massachusetts Institute of Technology. Department of Chemistry Hadley, Rose Currier Brophy, Megan Brunjes Gu, Yu Nakashige, Toshiki George Nolan, Elizabeth Marie |
| author_sort | Hadley, Rose Currier |
| collection | MIT |
| description | 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. |
| first_indexed | 2024-09-23T13:08:16Z |
| format | Article |
| id | mit-1721.1/125599 |
| institution | Massachusetts Institute of Technology |
| language | English |
| last_indexed | 2024-09-23T13:08:16Z |
| publishDate | 2020 |
| publisher | American Chemical Society (ACS) |
| record_format | dspace |
| spelling | mit-1721.1/1255992022-10-01T13:14:48Z Biochemical and Spectroscopic Observation of Mn(II) Sequestration from Bacterial Mn(II) Transport Machinery by Calprotectin Hadley, Rose Currier Brophy, Megan Brunjes Gu, Yu Nakashige, Toshiki George Nolan, Elizabeth Marie Massachusetts Institute of Technology. Department of Chemistry 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. National Institutes of Health (U.S.) (Grant R01GM118695) National Institutes of Health (U.S.) (Grant R01GM104543) National Science Foundation (U.S.) ( Grant 0070319) National Institutes of Health (U.S.) (Grant P30-ES002109) 2020-06-01T16:42:03Z 2020-06-01T16:42:03Z 2018-01 2020-01-02T15:56:55Z Article http://purl.org/eprint/type/JournalArticle 0002-7863 https://hdl.handle.net/1721.1/125599 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) en https://dx.doi.org/10.1021/JACS.7B11207 Journal of the American Chemical Society 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. application/pdf American Chemical Society (ACS) PMC |
| spellingShingle | Hadley, Rose Currier Brophy, Megan Brunjes Gu, Yu Nakashige, Toshiki George Nolan, Elizabeth Marie Biochemical and Spectroscopic Observation of Mn(II) Sequestration from Bacterial Mn(II) Transport Machinery by Calprotectin |
| title | Biochemical and Spectroscopic Observation of Mn(II) Sequestration from Bacterial Mn(II) Transport Machinery by Calprotectin |
| title_full | Biochemical and Spectroscopic Observation of Mn(II) Sequestration from Bacterial Mn(II) Transport Machinery by Calprotectin |
| title_fullStr | Biochemical and Spectroscopic Observation of Mn(II) Sequestration from Bacterial Mn(II) Transport Machinery by Calprotectin |
| title_full_unstemmed | Biochemical and Spectroscopic Observation of Mn(II) Sequestration from Bacterial Mn(II) Transport Machinery by Calprotectin |
| title_short | Biochemical and Spectroscopic Observation of Mn(II) Sequestration from Bacterial Mn(II) Transport Machinery by Calprotectin |
| title_sort | biochemical and spectroscopic observation of mn ii sequestration from bacterial mn ii transport machinery by calprotectin |
| url | https://hdl.handle.net/1721.1/125599 |
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