Isolation and characterization of a neprilysin-like protein from Venturia canescens virus-like particles

Insect Mol Biol. 2002 Oct;11(5):477-85. doi: 10.1046/j.1365-2583.2002.00356.x.

Abstract

Maternal protein secretions from endoparasitoid wasps are evolutionary adaptations to regulate host physiology as part of an extended wasp phenotype. Virus-like particles (VLPs) produced in the calyx region of Venturia canescens wasps are involved in immune evasion of the developing parasitoid inside the host. In contrast to polydnaviruses (PDVs), VcVLPs are devoid of any nucleic acids. To understand the role of these particles in the regulation of host physiology and phylogenetic relationship between VLPs and PDVs, it is essential to identify particle proteins. In this paper, we describe the isolation and molecular cloning of a neprilysin-like gene (VcNEP) coding for a 94 kDa VcVLP protein and discuss its possible role in host regulation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • DNA, Complementary
  • Humans
  • Insect Proteins / genetics*
  • Insect Viruses / enzymology*
  • Insect Viruses / genetics
  • Metalloendopeptidases / genetics*
  • Molecular Sequence Data
  • Neprilysin / genetics*
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid
  • Virion
  • Wasps / virology*

Substances

  • DNA, Complementary
  • Insect Proteins
  • Metalloendopeptidases
  • Neprilysin

Associated data

  • GENBANK/AF483275