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Cited by 72S100 Proteins and AnnexinsAntimicrobial Peptides and ActivitiesImmune Response and Inflammation

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S100 Proteins in the Innate Immune Response to Pathogens

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Kozlyuk, Natalia, Monteith, Andrew J., Garcia, Velia, Damo, Steven M., Skaar, Eric P., Chazin, Walter J.·2019·Methods in Molecular Biology
DOI 10.1007/978-1-4939-9030-6_18PMC PMC6475579
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Abstract

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.

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Metadata

Authors
Kozlyuk, N., Monteith, A. J., Garcia, V., Damo, S. M., Skaar, E. P., & Chazin, W. J.
Affiliations
  • Vanderbilt University (US)
  • Vanderbilt University Medical Center (US)
Corresponding author
Chazin, Walter J.
ORCID
Venue
Methods in Molecular Biology
Publisher
Springer New York
Published
2019
Volume
1929
Pages
275-290
ISSN
  • 1064-3745 (ISSN-L)
  • 1940-6029
DOI
10.1007/978-1-4939-9030-6_18
PMC
PMC6475579
OpenAlex
W2911456831
Cited by
72
References
12
Citations by year
2026: 8 · 2025: 5 · 2024: 9 · 2023: 14 · 2022: 12 · 2021: 10 · 2020: 10 · 2019: 3
FWCI
9.95
Type
book chapter
Language
en
Open access
Licence
www.springer.com/tdm (tdm)
Locations
  • Methods in molecular biology (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • National Heart, Lung, and Blood Institute (F32HL144081)
  • National Institute of General Medical Sciences (T32GM065086, T32GM008320)
  • National Institute of Allergy and Infectious Diseases (R01AI101171)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › S100 Proteins and Annexins
  • Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
  • Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
Keywords
S-100 protein, innate immunity, pathogen recognition, nutritional immunity, S100A7, S100A12, S100A8, S100A9, pattern recognition receptors, TLR4, RAGE, inflammation, antimicrobial activity, recombinant protein expression, binding affinity
MeSH terms
Calcium, Humans, Immunity, Innate, Inflammation, Manganese, Models, Molecular, S100 Proteins, Protein Conformation, Toll-Like Receptor 4, Host-Pathogen Interactions

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