Functional diversification upon leader protease domain duplication in the Citrus tristeza virus genome: Role of RNA sequences and the encoded proteins

Virology. 2018 Jan 15:514:192-202. doi: 10.1016/j.virol.2017.11.014. Epub 2017 Dec 1.

Abstract

Viruses from the family Closteroviridae show an example of intra-genome duplications of more than one gene. In addition to the hallmark coat protein gene duplication, several members possess a tandem duplication of papain-like leader proteases. In this study, we demonstrate that domains encoding the L1 and L2 proteases in the Citrus tristeza virus genome underwent a significant functional divergence at the RNA and protein levels. We show that the L1 protease is crucial for viral accumulation and establishment of initial infection, whereas its coding region is vital for virus transport. On the other hand, the second protease is indispensable for virus infection of its natural citrus host, suggesting that L2 has evolved an important adaptive function that mediates virus interaction with the woody host.

Keywords: Citrus tristeza virus; Gene duplication; Host range; Leader protease.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • 5' Untranslated Regions
  • Citrus / virology*
  • Closterovirus / enzymology*
  • Closterovirus / genetics
  • Closterovirus / physiology
  • Genome, Viral
  • Open Reading Frames
  • Peptide Hydrolases / genetics
  • Peptide Hydrolases / metabolism*
  • Plant Diseases / virology*
  • Protein Domains
  • RNA, Viral / genetics
  • RNA, Viral / metabolism
  • Viral Proteins / genetics
  • Viral Proteins / metabolism*

Substances

  • 5' Untranslated Regions
  • RNA, Viral
  • Viral Proteins
  • Peptide Hydrolases

Supplementary concepts

  • Citrus tristeza virus