Expression, Purification, and Antimicrobial Activity of S100A12
| Autor: | Jennifer A. Gaddy, Saffron R. Little, Steven M. Damo, Emmanuel Jackson, Dana Franklin |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
General Chemical Engineering chemistry.chemical_element Zinc Bacterial growth Biochemistry General Biochemistry Genetics and Molecular Biology Microbiology 03 medical and health sciences Anti-Infective Agents Immunity Calcium-binding protein Escherichia coli Calgranulin Humans Pathogen Innate immune system General Immunology and Microbiology biology Helicobacter pylori General Neuroscience S100A12 Protein Antimicrobial Immunity Innate 030104 developmental biology chemistry biology.protein Copper |
| Popis: | Calgranulin proteins are important mediators of innate immunity and are members of the S100 class of the EF-hand family of calcium binding proteins. Some S100 proteins have the capacity to bind transition metals with high affinity and effectively sequester them away from invading microbial pathogens in a process that is termed "nutritional immunity". S100A12 (EN-RAGE) binds both zinc and copper and is highly abundant in innate immune cells such as macrophages and neutrophils. We report a refined method for the expression, enrichment and purification of S100A12 in its active, metal-binding configuration. Utilization of this protein in bacterial growth and viability analyses reveals that S100A12 has antimicrobial activity against the bacterial pathogen, Helicobacter pylori. The antimicrobial activity is predicated on the zinc-binding activity of S100A12, which chelates nutrient zinc, thereby starving H. pylori which requires zinc for growth and proliferation. |
| Databáze: | OpenAIRE |
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