Proteins and Peptidases from Conidia and Mycelia of Scedosporium apiospermum Strain HLPB
| Autor: | Eliana Barreto-Bergter, Martha Machado Pereira, Bianca Alcântara da Silva, André L.S. Santos, Marcia R. Pinto |
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| Rok vydání: | 2008 |
| Předmět: |
Metallopeptidase
Veterinary (miscellaneous) Applied Microbiology and Biotechnology Microbiology Conidium Hemoglobins Albumins Gene Expression Regulation Fungal Humans Protease Inhibitors Scedosporium Mycelium biology fungi Mucins Proteolytic enzymes Albumin Scedosporium apiospermum Hydrogen-Ion Concentration Spores Fungal biology.organism_classification Fibronectins Pseudallescheria boydii Transformation (genetics) Biochemistry Immunoglobulin G Metalloproteases Laminin Agronomy and Crop Science Biomarkers Phenanthrolines |
| Zdroj: | Mycopathologia. 167:25-30 |
| ISSN: | 1573-0832 0301-486X |
| Popis: | The conidia-mycelia transformation is an essential step during the life cycle of the fungal human pathogens of the Pseudallescheria boydii complex. In the present study, we have analyzed the protein and peptidase profiles in two distinct morphological stages, conidia and mycelia, of Scedosporium apiospermum sensu stricto. Proteins synthesized by the mycelia, migrating at the ranges of 62-48 and 22-18 kDa, were not detected from the conidial extract. Conidia produced a single cellular peptidase of 28 kDa able to digest copolymerized albumin, while mycelia yielded 6 distinct peptidases ranging from 90 to 28 kDa. All proteolytic enzymes were active at acidic pH and fully inhibited by 1,10-phenanthroline, characterizing these activities as metallo-type peptidases. Quantitative peptidase assay, using soluble albumin, showed a high metallopeptidase production in mycelial cells in comparison with conidia. The regulated expression of proteins and peptidases in different morphological stages of S. apiospermum represents a potential target for isolation of stage-specific markers for biochemical and immunological analysis. |
| Databáze: | OpenAIRE |
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