Molecular cloning, characterization and tissue expression of prophenoloxidase cDNA from the mosquito Armigeres subalbatus inoculated with Dirofilaria immitis microfilariae

Insect Mol Biol. 1998 Feb;7(1):31-40. doi: 10.1046/j.1365-2583.1998.71049.x.

Abstract

A cDNA encoding mosquito Armigeres subalbatus prophenol oxidase (As-pro-PO) was obtained by rapid amplification of cDNA ends-polymerase chain reaction (RACE-PCR) after Dirofilaria immitis inoculation. The 2205 bp As-pro-PO cDNA contains a 32 bp 5'-noncoding region, a 2055 bp open reading frame (685 amino acids), and a 118 bp 3'-noncoding region. Hydrophobic signal peptide for the endoplasmic reticulum targeting is not found in the NH2-terminal region. Two potential copper-binding domains, amino acids 197-245 and 345-412, are highly homologous to those of the other insect pro-POs. A 2.2 kb As-pro-PO transcript was identified by Northern blot analysis using D. immitis microfilariae-inoculated A. subalbatus. Both in situ hybridization and Northern blot analysis demonstrated that As-pro-PO mRNA was synthesized in mosquito haemocytes but not in other tissues, i.e. fat bodies, midguts and ovaries, etc.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Blotting, Northern
  • Catechol Oxidase / genetics*
  • Cloning, Molecular
  • Culicidae / enzymology*
  • Culicidae / genetics
  • Culicidae / parasitology
  • DNA, Complementary
  • Dirofilaria immitis / physiology*
  • Dogs
  • Enzyme Precursors / genetics*
  • Female
  • In Situ Hybridization
  • Molecular Sequence Data
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid

Substances

  • DNA, Complementary
  • Enzyme Precursors
  • pro-phenoloxidase
  • Catechol Oxidase