title: Phosphorylation of Single Stranded RNA Virus Proteins and Potential for Novel Therapeutic Strategies.
abstract: Post translational modification of proteins is a critical requirement that regulates function. Among the diverse kinds of protein post translational modifications, phosphorylation plays essential roles in protein folding, protein:protein interactions, signal transduction, intracellular localization, transcription regulation, cell cycle progression, survival and apoptosis. Protein phosphorylation is also essential for many intracellular pathogens to establish a productive infection cycle. Preservation of protein phosphorylation moieties in pathogens in a manner that mirrors the host components underscores the co-evolutionary trajectory of pathogens and hosts, and sheds light on how successful pathogens have usurped, either in part or as a whole, the host enzymatic machinery. Phosphorylation of viral proteins for many acute RNA viruses including Flaviviruses and Alphaviruses has been demonstrated to be critical for protein functionality. This review focuses on phosphorylation modifications that have been documented to occur on viral proteins with emphasis on acutely infectious, single stranded RNA viruses. The review additionally explores the possibility of repurposing Food and Drug Administration (FDA) approved inhibitors as antivirals for the treatment of acute RNA viral infections.
authors.affiliation: National Center for Biodefense and Infectious Disease, School of Systems Biology, George Mason University, 10650 Pyramid Place, Manassas, VA 20110, USA. fkeck@masonlive.gmu.edu.
authors.forename: Forrest
authors.initials: F
authors.lastname: Keck
authors.affiliation: National Center for Biodefense and Infectious Disease, School of Systems Biology, George Mason University, 10650 Pyramid Place, Manassas, VA 20110, USA. pataey@gmu.edu.
authors.forename: Pouya
authors.initials: P
authors.lastname: Ataey
authors.affiliation: National Center for Biodefense and Infectious Disease, School of Systems Biology, George Mason University, 10650 Pyramid Place, Manassas, VA 20110, USA. mamaya3@gmu.edu.
authors.forename: Moushimi
authors.initials: M
authors.lastname: Amaya
authors.affiliation: National Center for Biodefense and Infectious Disease, School of Systems Biology, George Mason University, 10650 Pyramid Place, Manassas, VA 20110, USA. cbailey2@gmu.edu.
authors.forename: Charles
authors.initials: C
authors.lastname: Bailey
authors.affiliation: National Center for Biodefense and Infectious Disease, School of Systems Biology, George Mason University, 10650 Pyramid Place, Manassas, VA 20110, USA. anaraya1@gmu.edu.
authors.forename: Aarthi
authors.initials: A
authors.lastname: Narayanan
mesh_terms: D000818:Animals; D000998:Antiviral Agents / Q000378:metabolism / Q000627:therapeutic use; D054884:Host-Pathogen Interactions; D006801:Humans; D010766:Phosphorylation; D047428:Protein Kinase Inhibitors / Q000378:metabolism / Q000627:therapeutic use; D011499:Protein Processing, Post-Translational; D012328:RNA Viruses / Q000502:physiology*; D014764:Viral Proteins / Q000378:metabolism*
chemical_list: D000998:Antiviral Agents; D047428:Protein Kinase Inhibitors; D014764:Viral Proteins
keywords: antivirals; kinase; phosphorylation; post translational modification; therapeutics; viral protein