ArticleBiochemistry2020
Avian MRP126 Restricts Microbial Growth through Ca(II)-Dependent Zn(II) Sequestration.
Article in Biochemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 13 citations in OpenAlex.
- ExploitingFrontiers in immunology · 2026Article
- Evaluation of myeloid-related protein 126, cardiac troponin C and serum amyloid A as potential plasma biomarkers of health and disease in sea turtles.Conservation physiology · 2025Article
- Zebrafish do not have a calprotectin ortholog.PloS one · 2025Article
- Transcriptome and histological analyses on the uterus of freckle egg laying hens.BMC genomics · 2023Article
- Zinc in Human Health and Infectious Diseases.Biomolecules · 2022Review
- Dynamic regulation of Zn(II) sequestration by calgranulin C.Protein science : a publication of the Protein Society · 2022Article
- Review
- Molecular Evolution of Transition Metal Bioavailability at the Host-Pathogen Interface.Trends in microbiology · 2021Review
- Novel Models for Chronic Intestinal Inflammation in Chickens: Intestinal Inflammation Pattern and Biomarkers.Frontiers in immunology · 2021Article
- Evolution of multifunctionality through a pleiotropic substitution in the innate immune protein S100A9.eLife · 2020Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The calgranulins form a class of S100 proteins in higher vertebrates that innate-immune cells release in abundance at infection sites. These proteins function by binding transition metal ions to prevent microbial pathogens from obtaining those essential nutrients. Mammals express three distinct members of this family: S100A8 (calgranulin A), S100A9 (calgranulin B, which heterooligomerizes with S100A8 to form calprotectin), and S100A12 (calgranulin C), that exhibit Ca(II)-dependent transition metal binding properties. Human calprotectin effectively sequesters Mn(II), Fe(II), Ni(II), and Zn(II), whereas human S100A12 selectively sequesters Zn(II) over these other metal ions. Birds and reptiles express a single calgranulin homologue named MRP126, which we reasoned could have properties more similar to those of either calprotectin or S100A12. Here we present the purification and biophysical characterization of recombinant chicken MRP126 and, to the best of our knowledge, provide the first assessment of the metal binding and antimicrobial properties of an avian MRP126. We show that MRP126 is a homodimer that selectively sequesters Zn(II) and restricts the growth of certain microbes. MRP126 binds Zn(II) at two canonical His
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Registered trials
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