The involvement of heat shock proteins in the establishment of Tomato Yellow Leaf Curl Virus infection

Rena Gorovits, Henryk Czosnek*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

37 Scopus citations

Abstract

Tomato yellow leaf curl virus (TYLCV), a begomovirus, induces protein aggregation in infected tomatoes and in its whitefly vector Bemisia tabaci. The interactions between TYLCV and HSP70 and HSP90 in plants and vectors are necessity for virus infection to proceed. In infected host cells, HSP70 and HSP90 are redistributed from a soluble to an aggregated state. These aggregates contain, together with viral DNA/proteins and virions, HSPs and components of the protein quality control system such as ubiquitin, 26S proteasome subunits, and the autophagy protein ATG8. TYLCV CP can form complexes with HSPs in tomato and whitefly. Nonetheless, HSP70 and HSP90 play different roles in the viral cell cycle in the plant host. In the infected host cell, HSP70, but not HSP90, participates in the translocation of CP from the cytoplasm into the nucleus. Viral amounts decrease when HSP70 is inhibited, but increase when HSP90 is downregulated. In the whitefly vector, HSP70 impairs the circulative transmission of TYLCV; its inhibition increases transmission. Hence, the efficiency of virus acquisition by whiteflies depends on the functionality of both plant chaperones and their cross-talk with other protein mechanisms controlling virus-induced aggregation.

Original languageAmerican English
Article number355
JournalFrontiers in Plant Science
Volume8
DOIs
StatePublished - 16 Mar 2017

Bibliographical note

Publisher Copyright:
© 2017 Gorovits and Czosnek.

Keywords

  • Begomovirus
  • Heat shock proteins
  • Protein quality control
  • Tomato
  • Whitefly

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