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Biophysical characterization of prot...

Lee, Aaron P.

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Biophysical characterization of protein-protein and protein-RNA interactions important for the replication and pathogenicity of coronaviruses.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Biophysical characterization of protein-protein and protein-RNA interactions important for the replication and pathogenicity of coronaviruses./
Author:	Lee, Aaron P.
Description:	100 p.
Notes:	Source: Masters Abstracts International, Volume: 55-05.
Contained By:	Masters Abstracts International55-05(E).
Subject:	Biochemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=10112278
ISBN:	9781339754321

Biophysical characterization of protein-protein and protein-RNA interactions important for the replication and pathogenicity of coronaviruses.
Lee, Aaron P.

Biophysical characterization of protein-protein and protein-RNA interactions important for the replication and pathogenicity of coronaviruses. - 100 p.

Source: Masters Abstracts International, Volume: 55-05.

Thesis (M.S.)--Indiana University, 2016.

Coronaviruses (CoVs) are highly recombinogenic +-sense ssRNA viruses that employ template-switching or discontinuous transcription to replicate in cells, yielding a nested set of subgenomic (sg) RNA transcripts encoding structural and accessory proteins. Elucidating the mechanism by which CoVs transition from discontinuous to continuous transcription in order to make new viral particles is a long-term objective. We propose that protein-protein interactions mediated by the nucleocapsid (N) protein, and modulated by phosphorylation of a Ser/Arg-rich linker (SR-L) that connects the ssRNA-binding OB-fold-like N-terminal (NTD) and C-terminal (CTD) domains, is a key aspect of this transition. Unphosphorylated mouse hepatitis virus (MHV) N219 (NTD+SR-L) functions as a ssRNA chaperone and is capable of dissociating duplexes of the MHV transcriptional regulatory sequence (TRS), an activity linked to the viability of MHV via template-switching. Phosphomimetic N219 mutants have reduced RNA-binding and helix-destabilizing activity. Indeed, recent studies suggest that phosphorylation of the MHV N SR-L enhances an interaction with the cellular RNA helicase DDX1, driving a switch from discontinuous to continuous viral transcription. We show that these N219 phosphomimetic mutants enhance the DDX1 turnover in ssRNA (rA10 or rA19)-stimulated background, relative to unphosphorylated N219. Current work is focused on examining the impact of phosphomimetic N219s on N-stimulated helicase/translocase activity of DDX1. Additionally, CoVs must also replicate in a host background with innate and adaptive immune sensors designed to detect and clear the viral infection. Viruses have developed several strategies to proliferate in the host and evade detection. In a second project , we present biochemical experiments that provide support for the hypothesis that MERS-CoV accessory protein orf4a (NS3B) functions as dsRNA binding protein and an immune antagonist of type I interferon production.

ISBN: 9781339754321Subjects--Topical Terms:

518028
Biochemistry.

Biophysical characterization of protein-protein and protein-RNA interactions important for the replication and pathogenicity of coronaviruses.
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520 $a Coronaviruses (CoVs) are highly recombinogenic +-sense ssRNA viruses that employ template-switching or discontinuous transcription to replicate in cells, yielding a nested set of subgenomic (sg) RNA transcripts encoding structural and accessory proteins. Elucidating the mechanism by which CoVs transition from discontinuous to continuous transcription in order to make new viral particles is a long-term objective. We propose that protein-protein interactions mediated by the nucleocapsid (N) protein, and modulated by phosphorylation of a Ser/Arg-rich linker (SR-L) that connects the ssRNA-binding OB-fold-like N-terminal (NTD) and C-terminal (CTD) domains, is a key aspect of this transition. Unphosphorylated mouse hepatitis virus (MHV) N219 (NTD+SR-L) functions as a ssRNA chaperone and is capable of dissociating duplexes of the MHV transcriptional regulatory sequence (TRS), an activity linked to the viability of MHV via template-switching. Phosphomimetic N219 mutants have reduced RNA-binding and helix-destabilizing activity. Indeed, recent studies suggest that phosphorylation of the MHV N SR-L enhances an interaction with the cellular RNA helicase DDX1, driving a switch from discontinuous to continuous viral transcription. We show that these N219 phosphomimetic mutants enhance the DDX1 turnover in ssRNA (rA10 or rA19)-stimulated background, relative to unphosphorylated N219. Current work is focused on examining the impact of phosphomimetic N219s on N-stimulated helicase/translocase activity of DDX1. Additionally, CoVs must also replicate in a host background with innate and adaptive immune sensors designed to detect and clear the viral infection. Viruses have developed several strategies to proliferate in the host and evade detection. In a second project , we present biochemical experiments that provide support for the hypothesis that MERS-CoV accessory protein orf4a (NS3B) functions as dsRNA binding protein and an immune antagonist of type I interferon production.
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