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Journal of General Virology header logo

Volume 105, Issue 8

Arginyltransferase 1 (ATE1)-mediated proteasomal degradation of viral haemagglutinin protein: a unique host defence mechanism No Access

Graphical Abstract

Graphical abstract

Schematic representation of arginyltransferase 1 (ATE1)-mediated arginylation of cellular and haemagglutinin-neuraminidase (HN) protein.

Abstract

The extensive protein production in virus-infected cells can disrupt protein homeostasis and activate various proteolytic pathways. These pathways utilize post-translational modifications (PTMs) to drive the ubiquitin-mediated proteasomal degradation of surplus proteins. Protein arginylation is the least explored PTM facilitated by arginyltransferase 1 (ATE1) enzyme. Several studies have provided evidence supporting its importance in multiple physiological processes, including ageing, stress, nerve regeneration, actin formation and embryo development. However, its function in viral pathogenesis is still unexplored. The present work utilizes Newcastle disease virus (NDV) as a model to establish the role of the ATE1 enzyme and its activity in pathogenesis. Our data indicate a rise in levels of N-arginylated cellular proteins in the infected cells. Here, we also explore the haemagglutinin-neuraminidase (HN) protein of NDV as a presumable target for arginylation. The data indicate that the administration of Arg amplifies the arginylation process, resulting in reduced stability of the HN protein. ATE1 enzyme activity inhibition and gene expression knockdown studies were also conducted to analyse modulation in HN protein levels, which further substantiated the findings. Moreover, we also observed Arg addition and probable ubiquitin modification to the HN protein, indicating engagement of the proteasomal degradation machinery. Lastly, we concluded that the enhanced levels of the ATE1 enzyme could transfer the Arg residue to the N-terminus of the HN protein, ultimately driving its proteasomal degradation.

  • Received:
  • Accepted:
  • Published Online:
Keyword(s): arginylation , arginyltransferase 1 , haemagglutinin-neuraminidase protein , L-arginine , Newcastle disease virus and ubiquitination
Funding
This study was supported by the:
  • Board of Research in Nuclear Sciences (Award 58/14/05/2022)
    • Principle Award Recipient: DebapratimDas
  • Science and Engineering Research Board (Award CRG 2020/002030)
    • Principle Award Recipient: DebapratimDas
  • Indian Council of Medical Research (Award DDR/IIRP-23/2444)
    • Principle Award Recipient: SachinKumar
  • Department of Health Science (Award NER/71/2020-ECD-I)
    • Principle Award Recipient: SachinKumar
  • Rajiv Gandhi Centre for Biotechnology, Department of Biotechnology, Ministry of Science and Technology, India (Award BT/PR41246/NER/95/1685/2020)
    • Principle Award Recipient: SachinKumar
© 2024 The Authors
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2024-08-29
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Arginyltransferase 1 (ATE1)-mediated proteasomal degradation of viral haemagglutinin protein: a unique host defence mechanism
J. Gen. Virol. 105, 002020 (2024); https://doi.org/10.1099/jgv.0.002020
/content/journal/jgv/10.1099/jgv.0.002020
/content/journal/jgv/10.1099/jgv.0.002020
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