Brugia pahangi: identification and characterization of an aminopeptidase associated with larval molting

Exp Parasitol. 1993 Mar;76(2):127-33. doi: 10.1006/expr.1993.1015.

Abstract

The third-stage larvae (L3) of the filarid parasite Brugia pahangi were surveyed for protease activity beginning with release from the mosquito vector through molting to the fourth-stage larvae (L4). A metalloaminopeptidase with a substrate preference for phenylalanine was released during the molting process. A screen of aminopeptidase inhibitors identified H-boroPhenylalanine-(pinacol) as highly effective, with a Ki of 1.3 x 10(-11) M. This peptidase inhibitor also arrested molting of L3 larvae in vitro at a concentration of 100 microM.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Aminopeptidases / antagonists & inhibitors
  • Aminopeptidases / isolation & purification
  • Aminopeptidases / metabolism*
  • Animals
  • Boron Compounds / pharmacology
  • Brugia pahangi / enzymology*
  • Brugia pahangi / growth & development
  • Glycopeptides / pharmacology
  • Hydrogen-Ion Concentration
  • Larva / enzymology
  • Molecular Sequence Data
  • Molecular Weight
  • Oligopeptides / pharmacology
  • Phenylalanine / metabolism
  • Substrate Specificity

Substances

  • Boron Compounds
  • Glycopeptides
  • H-borophenylalanyl-(pinacol)
  • Oligopeptides
  • Phenylalanine
  • Aminopeptidases
  • phosphoramidon