Metal Sequestration and Antimicrobial Activity of Human Calprotectin Are pH-Dependent.
Journal
Biochemistry
ISSN: 1520-4995
Titre abrégé: Biochemistry
Pays: United States
ID NLM: 0370623
Informations de publication
Date de publication:
07 07 2020
07 07 2020
Historique:
pubmed:
4
6
2020
medline:
24
2
2021
entrez:
4
6
2020
Statut:
ppublish
Résumé
Human calprotectin (CP, S100A8/S100A9 oligomer) is an abundant innate immune protein that sequesters transition metal ions in the extracellular space to limit nutrient availability and the growth of invading microbial pathogens. Our current understanding of the metal-sequestering ability of CP is based on biochemical and functional studies performed at neutral or near-neutral pH. Nevertheless, CP can be present throughout the human body and is expressed at infection and inflammation sites that tend to be acidic. Here, we evaluate the metal binding and antimicrobial properties of CP in the pH range of 5.0-7.0. We show that Ca(II)-induced tetramerization, an important process for the extracellular functions of CP, is perturbed by acidic conditions. Moreover, a low pH impairs the antimicrobial activity of CP against some bacterial pathogens, including
Identifiants
pubmed: 32491853
doi: 10.1021/acs.biochem.0c00359
pmc: PMC7343615
mid: NIHMS1601283
doi:
Substances chimiques
Anti-Infective Agents
0
Leukocyte L1 Antigen Complex
0
Manganese
42Z2K6ZL8P
Calcium
SY7Q814VUP
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
2468-2478Subventions
Organisme : NIAID NIH HHS
ID : HHSN272200700055C
Pays : United States
Organisme : NIEHS NIH HHS
ID : P30 ES002109
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM126376
Pays : United States
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