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Nutritional Immunity: S100 Proteins at the Host-Pathogen Interface
Joseph P Zackular1, Walter J Chazin2, Eric P Skaar3
1From the Department of Pathology, Microbiology, and Immunology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232 and.
The Journal of Biological Chemistry
|June 10, 2015
Summary
Certain S100 proteins are crucial for the immune response, acting as antimicrobial agents. They employ nutritional immunity by limiting metal availability to fight infections.
Area of Science:
- Immunology
- Molecular Biology
- Biochemistry
Background:
- S100 proteins are EF-hand calcium-binding proteins vital for cellular functions.
- During infection, specific S100 proteins function as damage-associated molecular patterns (DAMPs).
- These S100 proteins interact with pattern recognition receptors, influencing inflammatory responses and pathogen defense.
Purpose of the Study:
- To review the role of S100 proteins in antimicrobial defense.
- To highlight S100 proteins that utilize nutritional immunity via metal limitation.
- To discuss recent advancements in understanding S100 protein-mediated metal sequestration during infection.
Main Methods:
- Literature review focusing on S100 proteins and antimicrobial properties.
- Analysis of S100 protein interactions with metal ions.
- Examination of S100 proteins in the context of nutritional immunity.
Main Results:
- S100 proteins possess potent antimicrobial properties.
- Nutritional immunity, through metal limitation, is a key antimicrobial mechanism for certain S100 proteins.
- S100 proteins sequester essential metals at infection sites, hindering pathogen growth.
Conclusions:
- S100 proteins are critical components of the innate immune system.
- Metal sequestration by S100 proteins represents a significant strategy in nutritional immunity.
- Further research into S100 protein-metal interactions can reveal new therapeutic targets for infectious diseases.
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