Histidine-Based Zinc-Binding Sequences and the Antimicrobial Activity of Calprotectin

Calprotectin is a protein in neutrophil cytoplasm and abscess fluids that appears to inhibit microbial growth through competition for zinc. This study was undertaken to identify specific sites that might be responsible for the protein's zinc-binding antimicrobial activity. A review of published...

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Bibliographic Details
Published in:The Journal of infectious diseases 1998-03, Vol.177 (3), p.812-814
Main Authors: Loomans, Henry J., Hahn, Beth L., Li, Qi-Qin, Phadnis, Suhas H., Sohnle, Peter G.
Format: Article
Language:English
Subjects:
Abscesses
Amino Acid Sequence
Amino acids
Antibiotics. Antiinfectious agents. Antiparasitic agents
Antifungal agents
Antifungal Agents - pharmacology
Antimicrobials
Binding Sites
Biological and medical sciences
Calcium binding proteins
Candida albicans - drug effects
Concise Communications
Fundamental and applied biological sciences. Psychology
Histidine
Leukocyte L1 Antigen Complex
Medical research
Medical sciences
Microbiology
Molecular Sequence Data
Mycology
Neural Cell Adhesion Molecules - pharmacology
Neutrophils
Pathogenicity, host-agent relations, miscellaneous strains, epidemiology
Pharmacology. Drug treatments
Proteins
Reagents
Structure-Activity Relationship
Yeasts
Zinc
Zinc - metabolism
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Summary:Calprotectin is a protein in neutrophil cytoplasm and abscess fluids that appears to inhibit microbial growth through competition for zinc. This study was undertaken to identify specific sites that might be responsible for the protein's zinc-binding antimicrobial activity. A review of published calprotectin amino acid sequences revealed the HEXXH motif of thermolysin-type metalloproteases and an HHH polyhistidine sequence near the C-terminus of the protein's heavy chain. Reagent polyhistidine had antimicrobial activity against Candida albicans similar to that of calprotectin. Also, one type of HEXXH-containing thermolysin was inactive in the C. albicans assay, whereas a protein tagged with six Cterminal histidines did have calprotectin-like zinc-reversible antimicrobial activity. The activity of polyhistidine, as well as that of calprotectin itself, was reversed by addition of zinc or treatment with the histidine-modifying compound diethylpyrocarbonate. These results suggest that calprotectin's antimicrobial activity may be related to certain histidine-based zinc-binding sequences.
ISSN:0022-1899
1537-6613
DOI:10.1086/517816