Rice stripe virus hitchhikes the vector insect vitellogenin ligand-receptor pathway for ovary entry

Philos Trans R Soc Lond B Biol Sci. 2019 Mar 4;374(1767):20180312. doi: 10.1098/rstb.2018.0312.

Abstract

It is known that plant arboviruses infect insect vector cells by endocytosis; however, the cellular receptors that mediate endocytosis have not been well defined. In our recently published work and this study, by clarifying the vertical transmission mechanism of Rice stripe virus (RSV) in Laodelphax striatellus, we provide a novel paradigm for how arboviruses enter insect germ-line cells. Instead of direct interaction with a viral receptor, the virus binds to a secreted ligand protein, hitchhiking the ligand-receptor pathway to achieve cell entry. Vitellogenin (Vg) is an indispensable protein for embryo development that is synthesized extra-ovarially and taken up by germ-line cells through Vg receptor (VgR)-mediated endocytosis. After revealing that RSV invades L. striatellus ovary by a specific molecular interaction with the insect Vg in haemolymph, this study addressed VgR's function in mediating the RSV invasion of the germarium nurse cells, further confirming the ligand's receptor-mediated viral cell-invasion mechanism. Understanding the viral ovary-entry pathways in vectors will help to find suitable measures to block the trans-generation transmission of the viruses. This article is part of the theme issue 'Biotic signalling sheds light on smart pest management'.

Keywords: anti-viral strategies; cellular receptor; insect vector; ligand-receptor pathway; plant arbovirus.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Egg Proteins / metabolism
  • Female
  • Hemiptera / genetics
  • Hemiptera / microbiology*
  • Insect Proteins / metabolism
  • Insect Vectors / genetics
  • Insect Vectors / microbiology*
  • Ligands
  • Oryza / virology*
  • Ovary / microbiology
  • Plant Diseases / microbiology*
  • Receptors, Cell Surface / metabolism
  • Tenuivirus / physiology*

Substances

  • Egg Proteins
  • Insect Proteins
  • Ligands
  • Receptors, Cell Surface
  • vitellogenin receptor

Associated data

  • figshare/10.6084/m9.figshare.c.4320986