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Purification and preliminary charact...

Mayer, Kendall M.

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Purification and preliminary characterization of key replicative accessory proteins from human coronaviruses.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Purification and preliminary characterization of key replicative accessory proteins from human coronaviruses./
Author:	Mayer, Kendall M.
Description:	101 p.
Notes:	Source: Masters Abstracts International, Volume: 54-04.
Contained By:	Masters Abstracts International54-04(E).
Subject:	Organic chemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=1588760
ISBN:	9781321749922

Purification and preliminary characterization of key replicative accessory proteins from human coronaviruses.
Mayer, Kendall M.

Purification and preliminary characterization of key replicative accessory proteins from human coronaviruses. - 101 p.

Source: Masters Abstracts International, Volume: 54-04.

Thesis (M.S.)--Indiana University, 2015.

Coronaviruses are RNA viruses that infect a variety of vertebrate hosts including humans. The coronavirus nucleocapsid (N) protein is a multifunctional protein proven to be important in infection, transcription, and virulence. N protein contains three distinct domains, an N terminal domain (NTD), a C terminal dimerization domain (CTD), and a serine and arginine rich linker (SR linker) between the NTD and CTD. The mouse hepatitis virus NTD and SR linker of N protein have previously been demonstrated to bind the N-terminal region of nonstructural protein3 (nsp3a), a part of the replicase-transcriptase complex (RTC). A new human coronavirus, middle east respiratory syndrome coronavirus (MERS-CoV) emerged in 2012. Nsp3a from MERS-CoV has been cloned and recombinantly expressed in E. coli. The protein is a suitable target for NMR and can be used to determine if the binding interaction is conserved in other coronaviruses. Immune evasion is another important aspect of RNA viruses. Nsp10 and Nsp16 are involved in 2'O-methylation of the cap on the 5' end of coronavirus RNA. This cap structure evades interferon induced genes that recognize viral RNA. Nsp10 from MERS has been cloned and recombinantly expressed in E. coli. To understand how it interacts with Nsp16, NMR can be used. The backbone of MERS Nsp10 has been assigned.

ISBN: 9781321749922Subjects--Topical Terms:

523952
Organic chemistry.

Purification and preliminary characterization of key replicative accessory proteins from human coronaviruses.
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245 1 0 $a Purification and preliminary characterization of key replicative accessory proteins from human coronaviruses.
300 $a 101 p.
500 $a Source: Masters Abstracts International, Volume: 54-04.
500 $a Adviser: David P. Giedroc.
502 $a Thesis (M.S.)--Indiana University, 2015.
520 $a Coronaviruses are RNA viruses that infect a variety of vertebrate hosts including humans. The coronavirus nucleocapsid (N) protein is a multifunctional protein proven to be important in infection, transcription, and virulence. N protein contains three distinct domains, an N terminal domain (NTD), a C terminal dimerization domain (CTD), and a serine and arginine rich linker (SR linker) between the NTD and CTD. The mouse hepatitis virus NTD and SR linker of N protein have previously been demonstrated to bind the N-terminal region of nonstructural protein3 (nsp3a), a part of the replicase-transcriptase complex (RTC). A new human coronavirus, middle east respiratory syndrome coronavirus (MERS-CoV) emerged in 2012. Nsp3a from MERS-CoV has been cloned and recombinantly expressed in E. coli. The protein is a suitable target for NMR and can be used to determine if the binding interaction is conserved in other coronaviruses. Immune evasion is another important aspect of RNA viruses. Nsp10 and Nsp16 are involved in 2'O-methylation of the cap on the 5' end of coronavirus RNA. This cap structure evades interferon induced genes that recognize viral RNA. Nsp10 from MERS has been cloned and recombinantly expressed in E. coli. To understand how it interacts with Nsp16, NMR can be used. The backbone of MERS Nsp10 has been assigned.
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