The insect metalloproteinase inhibitor gene of the lepidopteran Galleria mellonella encodes two distinct inhibitors
| Autor: | Christoph Weise, Marianne Wedde, Andreas Vilcinskas, Rolf Nuck, Boran Altincicek |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
Glycosylation
animal structures Matrix metalloproteinase inhibitor Molecular Sequence Data Clinical Biochemistry Thermolysin Matrix Metalloproteinase Inhibitors Matrix metalloproteinase Biochemistry Microbiology law.invention law Complementary DNA Animals Humans Amino Acid Sequence Molecular Biology Furin Peptide sequence Innate immune system Sequence Homology Amino Acid biology Reverse Transcriptase Polymerase Chain Reaction fungi Tissue Inhibitor of Metalloproteinases biology.organism_classification Recombinant Proteins Lepidoptera Galleria mellonella Matrix Metalloproteinase 9 Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization biology.protein Recombinant DNA Insect Proteins Electrophoresis Polyacrylamide Gel Matrix Metalloproteinase 1 |
| Zdroj: | Biological Chemistry. 388 |
| ISSN: | 1437-4315 1431-6730 |
| DOI: | 10.1515/bc.2007.013 |
| Popis: | The insect metalloproteinase inhibitor (IMPI) from the greater wax moth, Galleria mellonella, represents the first and to date only specific inhibitor of microbial metalloproteinases reported from animals. Here, we report on the characterization including carbohydrate analysis of two recombinant constructs encoded by impi cDNA either upstream or downstream of the furin cleavage site identified. rIMPI-1, corresponding to native IMPI purified from hemolymph, is encoded by the N-terminal part of the impi sequence, whereas rIMPI-2 is encoded by its C-terminal part. rIMPI-1 is glycosylated at N48 with GlcNAc2Man3, showing fucosylation to different extents. Similarly, rIMPI-2 is glycosylated at N149 with GlcNAc2Man3, but is fully fucosylated. rIMPI-1 represents a promising template for the design of second-generation antibiotics owing to its specific activity against thermolysin-like metalloproteinases produced by human pathogenic bacteria such as Vibrio vulnificus. In contrast, rIMPI-2 does not inhibit bacterial metalloproteinases, but is moderately active against recombinant human matrix metalloproteinases (MMPs). Both microbial metalloproteinases and MMPs induce expression of the impi gene when injected into G. mellonella larvae. These findings provide evidence that the impi gene encodes two distinct inhibitors, one inhibiting microbial metalloproteinases and contributing to innate immunity, the other putatively mediating regulation of endogenous MMPs during metamorphosis. |
| Databáze: | OpenAIRE |
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