Litcius/Paper detail

The C-Terminal Domains of the PB2 Subunit of the Influenza A Virus RNA Polymerase Directly Interact with Cellular GTPase Rab11a

Hana Veler, Haitian Fan, J.R. Keown, Jane Sharps, Marjorie Fournier, Jonathan M. Grimes, Ervin Fodor

2022Journal of Virology21 citationsDOIOpen Access PDF

Abstract

The influenza virus RNA genome segments are replicated in the cell nucleus and are assembled into viral ribonucleoprotein (vRNP) complexes with viral RNA polymerase and nucleoprotein (NP). Replicated vRNPs need to be exported from the nucleus and trafficked across the cytoplasm to the cell membrane, where virion assembly takes place. The host GTPase Rab11a plays a role in vRNP trafficking. In this study, we showed that the viral polymerase directly interacts with Rab11a mediating the interaction between vRNPs and Rab11a. We mapped this interaction to the C-terminal domains of the PB2 polymerase subunit and the switch I region of Rab11a. Identifying the exact site of Rab11a binding on the viral polymerase could uncover a novel target site for the development of an influenza antiviral drug.

Topics & Concepts

BiologyPolymeraseRibonucleoproteinCell biologyRNA polymeraseRNA polymerase IISmall nuclear RNAInfluenza A virusRNA-dependent RNA polymeraseRNA polymerase INuclear transportOrthomyxoviridaeMolecular biologyRNAVirologyCytoplasmCell nucleusBiochemistryVirusGeneGene expressionPromoterInfluenza Virus Research StudiesHIV Research and TreatmentBacteriophages and microbial interactions