Staphylococcal protein A is a novel heterologous substrate for the HIV-1 protease

Ilona Marczinovits, János Molnár, András Patthy

Research output: Article

3 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)79-83
Number of pages5
JournalJournal of Biotechnology
Issue number1
Publication statusPublished - szept. 15 1994

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

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