An antiviral protein from Bougainvillea spectabilis roots; purification and characterisation

Phytochemistry. 1998 Apr;47(8):1561-5. doi: 10.1016/s0031-9422(97)00788-7.

Abstract

An antiviral protein active against mechanical transmission of tomato spotted wilt virus was identified in the root tissues of Bougainvillea spectabilis Willd. Bougainvillea Antiviral Protein I (BAP I) was purified to apparent homogeneity from the roots of Bougainvillea by ammonium sulphate precipitation, CM- and DEAE-Sepharose chromatography and reverse phase HPLC. BAP I is a highly basic protein (pI value > 8.6) with an Mr of 28,000. The N-terminal sequence of BAP I showed homology with other plant antiviral proteins. Preliminary tests suggest that purified BAP I is capable of interfering with in vitro protein synthesis.

MeSH terms

  • Amino Acid Sequence
  • Antiviral Agents / chemistry
  • Antiviral Agents / isolation & purification*
  • Chromatography, High Pressure Liquid
  • Chromatography, Ion Exchange
  • Electrophoresis, Polyacrylamide Gel
  • Isoelectric Focusing
  • Molecular Sequence Data
  • Molecular Weight
  • Plant Proteins / chemistry
  • Plant Proteins / isolation & purification*
  • Plant Roots / chemistry*
  • Sequence Homology, Amino Acid

Substances

  • Antiviral Agents
  • BAPI protein, Bougainvillea spectabilis
  • Plant Proteins