Characteristics of acyrthosiphon pisum virus, a newly identified virus infecting the pea aphid

J Invertebr Pathol. 1997 Nov;70(3):169-76. doi: 10.1006/jipa.1997.4691.

Abstract

A new virus was isolated from the pea aphid, Acyrthosiphon pisum, and tentatively named Acyrthosiphon pisum virus (APV). The isometric virus particles were approximately 31 nm in diameter and contained a single-stranded RNA molecule of approximately 10 kb. Four structural proteins were observed with molecular masses of approximately 23.3, 24.2, 34.5, and 66.2 kDa. The 34.5-kDa capsid protein was the most abundant product in purified virions. Computer-assisted analysis revealed no significant homology between an internal sequence of 37 amino acids of the 34.5-kDa protein of APV and other polypeptides of viral origin. APV was not immunologically related to other ssRNA viruses from hemipteroid insects, such as aphid lethal paralysis virus, Rhopalosiphum padi virus, and Nezara viridula virus type 1. Immunolocalization on ultrathin sections of 3-day-old nymphs of A. pisum showed that APV antigen was predominantly present in the epithelial cells of the digestive tract. Virus particles were also observed associated with the microvilli of the intestine. Occasionally, muscle cells and mycetocyte cells were found infected. Purified APV, fed to 1-day-old A. pisum nymphs, significantly reduced the growth of the aphid and increased the time needed to reach maturity.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Aphids / virology*
  • Fabaceae / parasitology
  • Insect Viruses / genetics
  • Insect Viruses / pathogenicity*
  • Insect Viruses / ultrastructure
  • Molecular Sequence Data
  • Nymph / virology
  • Plants, Medicinal
  • RNA Viruses / genetics
  • RNA Viruses / pathogenicity*
  • RNA Viruses / ultrastructure
  • RNA, Viral / isolation & purification
  • Sequence Analysis
  • Sequence Homology, Amino Acid
  • Viral Structural Proteins / isolation & purification

Substances

  • RNA, Viral
  • Viral Structural Proteins