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Structural dynamics of a viral genom...

Ibrahim, Nouhou.

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Structural dynamics of a viral genomic RNA upon host protein binding.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Structural dynamics of a viral genomic RNA upon host protein binding./
Author:	Ibrahim, Nouhou.
Description:	124 p.
Notes:	Source: Masters Abstracts International, Volume: 47-06, page: 3412.
Contained By:	Masters Abstracts International47-06.
Subject:	Biology, Molecular. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=1465630
ISBN:	9781109238105

Structural dynamics of a viral genomic RNA upon host protein binding.
Ibrahim, Nouhou.

Structural dynamics of a viral genomic RNA upon host protein binding. - 124 p.

Source: Masters Abstracts International, Volume: 47-06, page: 3412.

Thesis (M.S.)--University of Nebraska at Omaha, 2009.

Coxsackieviruses, or CVBs, are responsible for a significant proportion of clinical myocarditis cases attributed to enterovirus infections. In addition to myocarditis, pancreatitis and possibly type I diabetes are caused by the Coxsackievirus serotype 3, or CVB3. CVB3 is a non-enveloped enterovirus of the Picornaviridae family. Its single-stranded, positive sense RNA genome is 7400 nucleotides long, and includes a 5' non-translated region (5'NTR), a single open reading frame, and a 3'NTR with a poly (A) tail. The local RNA structures within the CVB3 genome and particularly the internal ribosome entry site (IRES) within the 5'NTR are determinants for viral virulence. In fact, the IRES mediates cap-independent translation of the single open reading frame into a long polyprotein, which is then cleaved by viral proteases to produce mature viral proteins. The critical importance of the IRES relies on its ability to interact with viral and cellular proteins. IRES-transacting factors like the host poly (rC) binding protein 2 (or PCBP2) enhance 5'NTR activity. PCBP2 is known to regulate cellular mRNA stability and translation, but its commitment to the picornavirus life cycle depends on its affinity to C-rich regions of the 5'NTR resulting in translation enhancement and initiation of genome replication.

ISBN: 9781109238105Subjects--Topical Terms:

1017719
Biology, Molecular.

Structural dynamics of a viral genomic RNA upon host protein binding.
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020 $a 9781109238105
035 $a (UMI)AAI1465630
035 $a AAI1465630
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100 1 $a Ibrahim, Nouhou. $3 1669094
245 1 0 $a Structural dynamics of a viral genomic RNA upon host protein binding.
300 $a 124 p.
500 $a Source: Masters Abstracts International, Volume: 47-06, page: 3412.
500 $a Adviser: William E. Tapprich.
502 $a Thesis (M.S.)--University of Nebraska at Omaha, 2009.
520 $a Coxsackieviruses, or CVBs, are responsible for a significant proportion of clinical myocarditis cases attributed to enterovirus infections. In addition to myocarditis, pancreatitis and possibly type I diabetes are caused by the Coxsackievirus serotype 3, or CVB3. CVB3 is a non-enveloped enterovirus of the Picornaviridae family. Its single-stranded, positive sense RNA genome is 7400 nucleotides long, and includes a 5' non-translated region (5'NTR), a single open reading frame, and a 3'NTR with a poly (A) tail. The local RNA structures within the CVB3 genome and particularly the internal ribosome entry site (IRES) within the 5'NTR are determinants for viral virulence. In fact, the IRES mediates cap-independent translation of the single open reading frame into a long polyprotein, which is then cleaved by viral proteases to produce mature viral proteins. The critical importance of the IRES relies on its ability to interact with viral and cellular proteins. IRES-transacting factors like the host poly (rC) binding protein 2 (or PCBP2) enhance 5'NTR activity. PCBP2 is known to regulate cellular mRNA stability and translation, but its commitment to the picornavirus life cycle depends on its affinity to C-rich regions of the 5'NTR resulting in translation enhancement and initiation of genome replication.
520 $a The goal of this research was to provide evidence of interactions of PCBP2 with domain I and domain IV of the CVB3 5'NTR and to investigate potential structural dynamics within the 5'NTR upon PCBP2 binding. Our electrophoresis mobility shift assays (EMSA) using single RNA domains confirmed interaction between PCBP2 and domain IV, but not domain I. However, our structural studies using dimethylsylfate (DMS) modification within the context of the entire 5'NTR showed protection within domain IV as well as specific alterations of RNA secondary structures in domain I. Our results suggest a model in which simultaneous protection of RNA domains by PCBP2 trigger dynamic changes in 5'NTR structure.
590 $a School code: 1060.
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Biology, Microbiology. $3 1017734
650 4 $a Biology, Virology. $3 1019068
690 $a 0307
690 $a 0410
690 $a 0720
710 2 $a University of Nebraska at Omaha. $b Biology. $3 1669095
773 0 $t Masters Abstracts International $g 47-06.
790 1 0 $a Tapprich, William E., $e advisor
790 1 0 $a Swanson, Mark J. $e committee member
790 1 0 $a Kreiling, Jodi L. $e committee member
790 $a 1060
791 $a M.S.
792 $a 2009
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=1465630