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Assembly of a murine coronavirus.

Narayanan, Krishna.

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Assembly of a murine coronavirus.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Assembly of a murine coronavirus./
作者:	Narayanan, Krishna.
出版者:	Ann Arbor : ProQuest Dissertations & Theses, : 2001,
面頁冊數:	167 p.
附註:	Source: Dissertations Abstracts International, Volume: 63-02, Section: B.
Contained By:	Dissertations Abstracts International63-02B.
標題:	Microbiology. -
電子資源:	https://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3008404
ISBN:	9780493181394

Assembly of a murine coronavirus.
Narayanan, Krishna.

Assembly of a murine coronavirus. - Ann Arbor : ProQuest Dissertations & Theses, 2001 - 167 p.

Source: Dissertations Abstracts International, Volume: 63-02, Section: B.

Thesis (Ph.D.)--The University of Texas at Austin, 2001.

This item must not be sold to any third party vendors.

Mouse Hepatitis virus (MHV), a prototypic murine coronavirus, is an enveloped virus containing a single-stranded positive-sense RNA genome of approximately 31 kb. MHV contains three envelope proteins, M, E and S, and a nucleocapsid, that consists of genomic RNA and N protein, within the viral envelope. In infected cells, MHV produces a genome-length mRNA, mRNA 1, and 6-7 species of subgenomic mRNAs that form a 3' coterminal nested-set structure. Among these mRNAs, only the genomic-sized mRNA, mRNA 1, is efficiently packaged into MHV particles. According to the new model of coronavirus structure, MHV M protein exists in two different locations in the virus particle; on the viral envelope, and associated with a spherical core, inside the viral envelope. The present study examined whether M protein exists in two different locations in MHV particles. Characterization of MHV particles, after protease digestion, demonstrated that M protein existed only on the viral envelope, and not inside the virus particle. Removal of MHV envelope, with a non-ionic detergent under different conditions of salt concentration, followed by coimmunoprecipitation analysis demonstrated the presence of an ionic interaction between M protein and the N protein-genomic RNA complex in MHV particles. We also examined the macromolecular interactions involved in the envelopment of nucleocapsid in infected cells. Coimmunoprecipitation analyses demonstrated a specific interaction between N protein and M protein, in a pre-Golgi compartment, and also revealed that while N protein interacted with all MHV mRNAs, M protein interacted with only genomic-length MHV mRNA, mRNA 1, in infected cells. These data indicated that M protein specifically interacted with the nucleocapsid, consisting of N protein and mRNA 1, in infected cells. However, M protein-N protein interaction did not occur in cells coexpressing M protein and N protein alone, indicating that some MHV function(s) was necessary for the initiation of M protein-nucleocapsid interaction. The M protein-nucleocapsid interaction, which occurred near or at the MHV budding site, most probably represented the process of specific packaging of MHV genome into MHV particles. Previous studies have shown that a short cis-acting MHV RNA packaging signal is necessary and sufficient for packaging RNA into MHV particles. The present study examined the mechanism by which the packaging signal determines the selective packaging of RNAs into MHV particles. Regardless of the presence or absence of the packaging signal, N protein bound to MHV defective interfering RNAs and intracellularly expressed non-MHV RNA transcripts to form ribonucleoprotein complexes. M protein, however, interacted selectively with RNAs containing the packaging signal and only those RNAs, that interacted selectively with M protein, were efficiently packaged into MHV particles. Thus, the packaging signal mediated a selective interaction between M protein and viral RNA to drive the specific packaging of RNA into virus particles.

ISBN: 9780493181394Subjects--Topical Terms:

536250
Microbiology.
Subjects--Index Terms:

Coronavirus

Assembly of a murine coronavirus.
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520 $a Mouse Hepatitis virus (MHV), a prototypic murine coronavirus, is an enveloped virus containing a single-stranded positive-sense RNA genome of approximately 31 kb. MHV contains three envelope proteins, M, E and S, and a nucleocapsid, that consists of genomic RNA and N protein, within the viral envelope. In infected cells, MHV produces a genome-length mRNA, mRNA 1, and 6-7 species of subgenomic mRNAs that form a 3' coterminal nested-set structure. Among these mRNAs, only the genomic-sized mRNA, mRNA 1, is efficiently packaged into MHV particles. According to the new model of coronavirus structure, MHV M protein exists in two different locations in the virus particle; on the viral envelope, and associated with a spherical core, inside the viral envelope. The present study examined whether M protein exists in two different locations in MHV particles. Characterization of MHV particles, after protease digestion, demonstrated that M protein existed only on the viral envelope, and not inside the virus particle. Removal of MHV envelope, with a non-ionic detergent under different conditions of salt concentration, followed by coimmunoprecipitation analysis demonstrated the presence of an ionic interaction between M protein and the N protein-genomic RNA complex in MHV particles. We also examined the macromolecular interactions involved in the envelopment of nucleocapsid in infected cells. Coimmunoprecipitation analyses demonstrated a specific interaction between N protein and M protein, in a pre-Golgi compartment, and also revealed that while N protein interacted with all MHV mRNAs, M protein interacted with only genomic-length MHV mRNA, mRNA 1, in infected cells. These data indicated that M protein specifically interacted with the nucleocapsid, consisting of N protein and mRNA 1, in infected cells. However, M protein-N protein interaction did not occur in cells coexpressing M protein and N protein alone, indicating that some MHV function(s) was necessary for the initiation of M protein-nucleocapsid interaction. The M protein-nucleocapsid interaction, which occurred near or at the MHV budding site, most probably represented the process of specific packaging of MHV genome into MHV particles. Previous studies have shown that a short cis-acting MHV RNA packaging signal is necessary and sufficient for packaging RNA into MHV particles. The present study examined the mechanism by which the packaging signal determines the selective packaging of RNAs into MHV particles. Regardless of the presence or absence of the packaging signal, N protein bound to MHV defective interfering RNAs and intracellularly expressed non-MHV RNA transcripts to form ribonucleoprotein complexes. M protein, however, interacted selectively with RNAs containing the packaging signal and only those RNAs, that interacted selectively with M protein, were efficiently packaged into MHV particles. Thus, the packaging signal mediated a selective interaction between M protein and viral RNA to drive the specific packaging of RNA into virus particles.
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