Zinc‐Reversible Antimicrobial Activity of Recombinant Calprotectin (Migration Inhibitory Factor–Related Proteins 8 and 14)
| Autor: | Walter J. Chazin, Michael J. Hunter, Peter G. Sohnle, Beth L. Hahn |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
Antifungal Agents
Peptide Microbial Sensitivity Tests Biology law.invention Structure-Activity Relationship chemistry.chemical_compound law Candida albicans Calgranulin B Immunology and Allergy Calgranulin A Amino Acid Sequence Neural Cell Adhesion Molecules Peptide sequence chemistry.chemical_classification Membrane Glycoproteins Calcium-Binding Proteins S100 Proteins Biological activity Antimicrobial biology.organism_classification Antigens Differentiation Recombinant Proteins Zinc Infectious Diseases chemistry Biochemistry Recombinant DNA Calprotectin Growth inhibition Leukocyte L1 Antigen Complex |
| Zdroj: | The Journal of Infectious Diseases. 182:1272-1275 |
| ISSN: | 1537-6613 0022-1899 |
| DOI: | 10.1086/315810 |
| Popis: | Recombinant calprotectin, consisting of 2 individual peptide chains also called migration inhibitory factor-related protein (MRP)-8 and MRP14, was tested for antimicrobial activity in a Candida albicans growth inhibition assay. Both chains contain HEXXH zinc-binding sites and might be expected to manifest zinc-reversible, antimicrobial activity similar to that of native calprotectin. When tested alone, neither MRP8 nor MRP14 showed activity in the Candida growth assay. A synthetic 20-amino acid peptide containing the HEXXH sequence of MRP14, along with a nearby HHH sequence, was also inactive in this assay. However, equimolar concentrations of MRP8 and MRP14 demonstrated a potent growth inhibitory effect that was reversible by 30 microM zinc. Truncated MRP14 (missing the C-terminal GHHHKPGLGEGTP tail) used in combination with MRP8 demonstrated zinc-reversible activity that was somewhat less than that with complete MRP14. These results suggest that intact calprotectin, consisting of a heterodimer of MRP8 and MRP14, is necessary to form a zinc-binding site capable of inhibiting microbial growth. |
| Databáze: | OpenAIRE |
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