The Glycolytic Pyruvate Kinase Is Recruited Directly into the Viral Replicase Complex to Generate ATP for RNA Synthesis

Chingkai Chuang, K. Reddisiva Prasanth, Peter D. Nagy

Research output: Contribution to journalArticle

10 Scopus citations


Viruses accomplish their replication by exploiting many cellular resources, including metabolites and energy. Similarly to other (+)RNA viruses, tomato bushy stunt virus (TBSV) induces major changes in infected cells. However, the source of energy required to fuel TBSV replication is unknown. We find that TBSV co-opts the cellular glycolytic ATP-generating pyruvate kinase (PK) directly into the viral replicase complex to boost progeny RNA synthesis. The co-opted PK generates high levels of ATP within the viral replication compartment at the expense of a reduction in cytosolic ATP pools. The ATP generated by the co-opted PK is used to promote the helicase activity of recruited cellular DEAD-box helicases, which are involved in the production of excess viral (+)RNA progeny. Altogether, recruitment of PK and local production of ATP within the replication compartment allow the virus replication machinery an access to plentiful ATP, facilitating robust virus replication. RNA viruses co-opt several host proteins to aid their replication in infected cells. Chuang et al. demonstrate that a small plant virus recruits the cellular glycolytic pyruvate kinase (PK) directly into the viral replicase complex. PK supplies ATP to fuel co-opted cellular helicases, which drives rapid viral RNA synthesis.

Original languageEnglish (US)
Pages (from-to)639-652.e7
JournalCell Host and Microbe
Issue number5
StatePublished - Nov 8 2017
Externally publishedYes



  • DEAD-box helicase
  • glycolysis
  • intracellular ATP biosensor
  • plant
  • RNA virus
  • RPN11 deubiquitinase
  • tomato bushy stunt virus
  • viral replication complex
  • virus replication
  • yeast

ASJC Scopus subject areas

  • Parasitology
  • Microbiology
  • Virology

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