S100 Proteins in the Innate Immune Response to Pathogens
Autor: | Andrew J. Monteith, Natalia Kozlyuk, Eric P. Skaar, Velia Garcia, Walter J. Chazin, Steven M. Damo |
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Rok vydání: | 2019 |
Předmět: |
Models
Molecular 0301 basic medicine Protein Conformation Host–pathogen interaction Inflammation Article RAGE (receptor) 03 medical and health sciences 0302 clinical medicine Immunity Protein purification medicine Humans Receptor Manganese Innate immune system Chemistry S100 Proteins Pattern recognition receptor Immunity Innate Cell biology Toll-Like Receptor 4 030104 developmental biology 030220 oncology & carcinogenesis Host-Pathogen Interactions Calcium medicine.symptom |
Zdroj: | Methods in Molecular Biology ISBN: 9781493990290 |
Popis: | S100 proteins are distinct dimeric EF-hand Ca(2+)-binding proteins that can bind Zn(2+), Mn(2+), and other transition metals with high affinity at two sites in the dimer interface. Certain S100 proteins, including S100A7, S100A12, S100A8, and S100A9, play key roles in the innate immune response to pathogens. These proteins function via a “nutritional immunity” mechanism by depleting essential transition metals in the infection that are required for the invading organism to grow and thrive. They also act as damage-associated molecular pattern ligands, which activate pattern recognition receptors (e.g., Toll-like receptor 4 RAGE) that mediate inflammation. Here we present protocols for these S100 proteins for high-level production of recombinant protein, measurement of binding affinities using isothermal titration calorimetry, and an assay of antimicrobial activity. |
Databáze: | OpenAIRE |
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