Purification and characterisation of a protease inhibitor from Streptomyces chromofuscus 34-1 with an antiviral activity

Biochim Biophys Acta. 2006 Aug;1760(8):1210-6. doi: 10.1016/j.bbagen.2006.03.002. Epub 2006 Mar 24.

Abstract

The aim of this study was to purify and characterise a novel protease inhibitor (PISC-2002) isolated from culture supernatants of Streptomyces chromofuscus. PISC-2002 was purified by anion-exchange chromatography, and RP-HPLC analysis. PISC-2002 had a molecular mass of 11.2 kDa and a high content of hydrophobic amino acids and proline. N-terminal sequence gave two sequences differing by one residue. The main sequence is ASLPAVSALVLTV and the shorter sequence is SLPAVSALVLTV. This shows its homology to Streptomyces subtilisin inhibitor family. Besides its large spectrum of powerful inhibitory activities against various serine proteases, PISC-2002 displayed significant antiviral effect against influenza virus A/Rostock/34 (H7N7).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Antiviral Agents / pharmacology*
  • Chromatography, High Pressure Liquid
  • Electrophoresis, Polyacrylamide Gel
  • Influenza A Virus, H7N7 Subtype / drug effects
  • Microbial Sensitivity Tests
  • Molecular Sequence Data
  • Protease Inhibitors / chemistry*
  • Protease Inhibitors / isolation & purification*
  • Protease Inhibitors / pharmacology*
  • Streptomyces / chemistry*

Substances

  • Antiviral Agents
  • Protease Inhibitors