Selective modification of Sendai virus hemagglutinin neuraminidase by pyridoxal 5'-phosphate: evidence for an allosteric modulation of neuraminidase activity

Biochim Biophys Acta. 1993 Feb 13;1161(2-3):323-7. doi: 10.1016/0167-4838(93)90232-g.

Abstract

Incubation of Sendai virus with pyridoxal 5'-phosphate (PLP) causes inhibition of hemolytic activity, a slight reduction of hemagglutinating activity, and an increase in neuraminidase activity. The effects on hemagglutination and neuraminidase are prevented by the presence in the incubation mixture of sialyl lactose, a substrate of hemagglutinin-neuraminidase. Incubation with PLP of the water-soluble enzymatic domain of the neuraminidase has no effect on enzymatic activity, while the allosteric inhibition (Dallocchio et al. (1991) Biochem. Int. 25, 663-668) disappears. Both virus-bound and solubilized neuraminidase are selectively modified by PLP at the lysine-553. Our data suggest that PLP inactivates a previously undetected inhibitory site on the viral neuraminidase, and that a physiological effector is present on the viral envelope.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allosteric Regulation
  • Amino Acids / analysis
  • Chromatography, High Pressure Liquid
  • HN Protein / chemistry
  • HN Protein / metabolism*
  • Hemagglutination, Viral
  • Humans
  • Lysine / metabolism
  • Parainfluenza Virus 1, Human / enzymology*
  • Pyridoxal Phosphate / metabolism*
  • Substrate Specificity

Substances

  • Amino Acids
  • HN Protein
  • Pyridoxal Phosphate
  • Lysine