Purification and characterization of a Laccase with inhibitory activity toward HIV-1 reverse transcriptase and tumor cells from an edible mushroom (Pleurotus cornucopiae)

Protein Pept Lett. 2010 Aug;17(8):1040-7. doi: 10.2174/092986610791498966.

Abstract

A 66-kDa laccase, with an N-terminal sequence different from those of other mushroom laccases, was purified from fresh fruiting bodies of the edible mushroom Pleurotus cornucopiae by using affinity chromatography on Affi-gel blue gel, ion exchange chromatography on Mono Q and gel filtration on Superdex 75. The procedure resulted in a 16-fold purification and a specific enzyme activity of 17.3 U mg(-1). The optimum pH and temperature for the purified laccase were pH 4 and 40 degrees C, respectively. This laccase inhibited proliferation of murine leukemia cell line L1210 and human hepatoma cell line HepG2, and reduced the activity of HIV-1 reverse transcriptase with an IC50 of 22 microM. There was neither mitogenic activity toward mouse splenocytes, nor hemagglutinating/hemolytic activity toward rabbit erythrocytes. This study yielded information about the potentially exploitable activities of P. cornucopiae laccase.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Proliferation / drug effects
  • Cells, Cultured
  • HIV Reverse Transcriptase / antagonists & inhibitors*
  • HIV-1 / drug effects
  • HIV-1 / enzymology*
  • Humans
  • Laccase / chemistry
  • Laccase / isolation & purification
  • Laccase / metabolism*
  • Laccase / pharmacology
  • Mice
  • Mice, Inbred C57BL
  • Pleurotus / enzymology*
  • Rabbits
  • Reverse Transcriptase Inhibitors / isolation & purification
  • Reverse Transcriptase Inhibitors / metabolism*
  • Reverse Transcriptase Inhibitors / pharmacology

Substances

  • Reverse Transcriptase Inhibitors
  • Laccase
  • reverse transcriptase, Human immunodeficiency virus 1
  • HIV Reverse Transcriptase