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Bioessays. 2017 Oct;39(10). doi: 10.1002/bies.201700014. Epub 2017 Sep 8.

Prenylation of viral proteins by enzymes of the host: Virus-driven rationale for therapy with statins and FT/GGT1 inhibitors.

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School of Systems Biology, George Mason University, Fairfax, VA, USA.
Bioinformatics Institute, Agency for Science, Technology and Research, Singapore.
Department of Biological Sciences, National University Singapore, Singapore.
School of Computer Engineering, Nanyang Technological University, Singapore.
Research Centre for Medical Genetics, Russian Academy of Medical Sciences, Moscow, Russia.


Intracellular bacteria were recently shown to employ eukaryotic prenylation system for modifying activity and ensuring proper intracellular localization of their own proteins. Following the same logic, the proteins of viruses may also serve as prenylation substrates. Using extensively validated high-confidence prenylation predictions by PrePS with a cut-off for experimentally confirmed farnesylation of hepatitis delta virus antigen, we compiled in silico evidence for several new prenylation candidates, including IRL9 (CMV) and few other proteins encoded by Herpesviridae, Nef (HIV-1), E1A (human adenovirus 1), NS5A (HCV), PB2 (influenza), HN (human parainfluenza virus 3), L83L (African swine fever), MC155R (molluscum contagiosum virus), other Poxviridae proteins, and some bacteriophages of human associated bacteria. If confirmed experimentally, these findings may aid in dissection of molecular functions of uncharacterized viral proteins and provide a novel rationale for statin and FT/GGT1-based inhibition of viral infections. Prenylation of bacteriophage proteins may aid in moderation of microbial infections.


CAAX; PrePS; bacteriophages; human viruses; protein prenylation

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