Identification and Characterization of Spodoptera frugiperda Furin: A Thermostable Subtilisin-Like Endoprotease
Autor: | Michael Cieplik, Hans-Dieter Klenk, Wolfgang Garten |
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Rok vydání: | 1998 |
Předmět: |
DNA
Complementary Serine Proteinase Inhibitors animal structures viruses Molecular Sequence Data Clinical Biochemistry Hemagglutinins Viral Sf9 Spodoptera Biochemistry law.invention Plasmid law Complementary DNA Enzyme Stability parasitic diseases Animals Amino Acid Sequence Cysteine Subtilisins Cloning Molecular Molecular Biology Furin Base Sequence Sequence Homology Amino Acid biology Chemistry Hydrolysis fungi Temperature Subtilisin Hydrogen-Ion Concentration biology.organism_classification Proprotein convertase Nucleopolyhedroviruses Influenza A virus embryonic structures Recombinant DNA biology.protein Calcium Cattle |
Zdroj: | bchm. 379:1433-1440 |
ISSN: | 1437-4315 1431-6730 |
DOI: | 10.1515/bchm.1998.379.12.1433 |
Popis: | Spodoptera frugiperda (Sf9) cells are widely employed for high-level expression of heterologous recombinant genes from baculovirus vectors. Using a plasmid library encoding cDNA of Sf9 cells we have identified here the Spodoptera frugiperda analog of the proprotein convertase furin which plays an important role in posttranslational protein processing. Spodoptera frugiperda furin (Sfurin) is closest related to Drosophila melanogasterfurin with which it shares an extended cysteine-rich domain, whereas mammalian furin shows high homology only in the catalytic domain. Mammalian furin and Sfurin were further compared by expression from baculovirus vectors. Substrate specificity and inhibitor profiles are identical for Sfurin and mammalian furin, whereas calcium-dependence, pH-optimum, and thermostability differ. Cleavage of recombinant influenza virus hemagglutinin was significantly enhanced in Sf9 cells after overexpression of Sfurin. |
Databáze: | OpenAIRE |
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