Phosphorylation of human respiratory syncytial virus P protein at serine 54 regulates viral uncoating

Virology
A AsenjoN Villanueva

Abstract

The human respiratory syncytial virus (HRSV) structural P protein, phosphorylated at serine (S) and threonine (T) residues, is a co-factor of viral RNA polymerase. The phosphorylation of S54 is controlled by the coordinated action of two cellular enzymes: a lithium-sensitive kinase, probably glycogen synthetase kinase (GSK-3) beta and protein phosphatase 2A (PP2A). Inhibition of lithium-sensitive kinase, soon after infection, blocks the viral growth cycle by inhibiting synthesis and/or accumulation of viral RNAs, proteins and extracellular particles. P protein phosphorylation at S54 is required to liberate viral ribonucleoproteins (RNPs) from M protein, during the uncoating process. Kinase inhibition, late in infection, produces a decrease in genomic RNA and infectious viral particles. LiCl, intranasally applied to mice infected with HRSV A2 strain, reduces the number of mice with virus in their lungs and the virus titre. Administration of LiCl to humans via aerosol should prevent HRSV infection, without secondary effects.

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Citations

Dec 22, 2009·Future Microbiology·Sandra M FuentesBiao He
Nov 26, 2010·Journal of Virology·Angela Vázquez-CalvoMiguel A Martín-Acebes
Mar 26, 2016·Frontiers in Microbiology·Ana B BlázquezJuan-Carlos Saiz
Apr 19, 2019·Journal of Virology·Justyna BroniarczykLawrence Banks
Apr 26, 2018·Mini Reviews in Medicinal Chemistry·Paulo André Teixeira De Moraes GomesAna C Lima Leite
Jun 12, 2020·Drug Development Research·Ravi Philip Rajkumar

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