Staphylococcal protein A is a novel heterologous substrate for the HIV-1 protease
| Autor: | András Patthy, János Molnár, Ilona Marczinovits |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Vesicle-associated membrane protein 8
Binding Sites biology Molecular Sequence Data Bioengineering General Medicine Applied Microbiology and Biotechnology Molecular biology Fusion protein Peptide Fragments Substrate Specificity Retinoblastoma-like protein 1 DDB1 HIV Protease HSPA2 SNAP23 Protein A/G HIV-1 biology.protein Electrophoresis Polyacrylamide Gel Amino Acid Sequence Protein G Staphylococcal Protein A Plasmids Biotechnology |
| Zdroj: | Journal of Biotechnology. 37:79-83 |
| ISSN: | 0168-1656 |
| Popis: | Upon in vitro processing of the recombinant HIV-1/gag p24 protein, expressed in Escherichia coli as a fusion protein, by HIV-1 protease, a cleavage site within the staphylococcal protein A fusion partner was found. N-terminal sequencing of the protein A fragments showed that HIV-1 protease cleavage occurred between phenylalanine-235 and tyrosine-236 within the sequence Gln-Asn-Ala-Phe/Tyr-Glu-Ile-Leu (QNAF/YEIL) in the IgG-binding domain C of the protein A encoded by the pRIT2T fusion gene vector (Pharmacia). Results presented here have proven that the protease-sensitive site is viable in vitro on the protein A alone and other chimeric protein, protein A/β-galactosidase. A possible significance of this phenomenon in biotechnology work is discussed. |
| Databáze: | OpenAIRE |
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