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Reovirus Core Proteins Play Roles in Disassembly and Early Replication.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Reovirus Core Proteins Play Roles in Disassembly and Early Replication./
作者:	Gummersheimer, Stephanie L.
出版者:	Ann Arbor : ProQuest Dissertations & Theses, : 2022,
面頁冊數:	130 p.
附註:	Source: Dissertations Abstracts International, Volume: 83-12, Section: B.
Contained By:	Dissertations Abstracts International83-12B.
標題:	Microbiology. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=29168976
ISBN:	9798819325711

Reovirus Core Proteins Play Roles in Disassembly and Early Replication.
Gummersheimer, Stephanie L.

Reovirus Core Proteins Play Roles in Disassembly and Early Replication. - Ann Arbor : ProQuest Dissertations & Theses, 2022 - 130 p.

Source: Dissertations Abstracts International, Volume: 83-12, Section: B.

Thesis (Ph.D.)--Indiana University, 2022.

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

Dissassembly of viral outer capsid is a critical step for successful infection of host cells. Mammalian orthoreovirus (reovirus) particles unable to complete disassembly steps upon entry have significantly reduced infectivity. Reovirus capsids contain two concentric protein shells that protect a segmented dsRNA genome. The outer capsid layer is composed of trimers of μ1 capped with σ3. The inner layer or core is composed of decamers of λ1 stabilized by the clamp-like protein σ2. After entry into host cells, σ3 is proteolytically degraded and μ1 is cleaved resulting in the formation of infectious subvirion particles or ISVPs. Further conformational changes in the capsid proteins result in the formation of a second disassembly intermediate, the ISVP*. Previous work to characterize these disassembly intermediates has focused on changes and interactions between the outer capsid proteins. My work aims to examine the contributions of the core proteins to the disassembly process. To do this, we generated a series of reassortant viruses containing primarily gene segments from a type 3 reovirus except for the gene segments coding for core proteins λ1 and σ2 (L3 and S2 respectively) which came from a type 1 virus. To determine the residues important for interactions between the core and the outer capsid that could be contributing to this phenotype, we used two approaches. First, we screened for viruses that accumulated mutations that generate hyperstable ISVPs. Through this screen, we did not isolate residues in the core proteins important for these interactions but instead identified several amino acid residues in the μ1 ϕ region that had not been previously associated with ISVP stability. Our second approach focused on targeting specific amino acids residues in the core proteins that vary between type 3 and type 1 serotypes. We generated viruses with chimeric λ1 proteins or with point mutations in σ2. Via this method, we determined specific changes in the core proteins that reduced the stability of ISVPs. Additionally, using these specifically generated mutants, we identified regions λ1 and σ2 that affect events in viral replication distinct from entry. These data highlight the multiple roles for capsid proteins during infection.

ISBN: 9798819325711Subjects--Topical Terms:

536250
Microbiology.
Subjects--Index Terms:

Capsids

Reovirus Core Proteins Play Roles in Disassembly and Early Replication.
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520 $a Dissassembly of viral outer capsid is a critical step for successful infection of host cells. Mammalian orthoreovirus (reovirus) particles unable to complete disassembly steps upon entry have significantly reduced infectivity. Reovirus capsids contain two concentric protein shells that protect a segmented dsRNA genome. The outer capsid layer is composed of trimers of μ1 capped with σ3. The inner layer or core is composed of decamers of λ1 stabilized by the clamp-like protein σ2. After entry into host cells, σ3 is proteolytically degraded and μ1 is cleaved resulting in the formation of infectious subvirion particles or ISVPs. Further conformational changes in the capsid proteins result in the formation of a second disassembly intermediate, the ISVP*. Previous work to characterize these disassembly intermediates has focused on changes and interactions between the outer capsid proteins. My work aims to examine the contributions of the core proteins to the disassembly process. To do this, we generated a series of reassortant viruses containing primarily gene segments from a type 3 reovirus except for the gene segments coding for core proteins λ1 and σ2 (L3 and S2 respectively) which came from a type 1 virus. To determine the residues important for interactions between the core and the outer capsid that could be contributing to this phenotype, we used two approaches. First, we screened for viruses that accumulated mutations that generate hyperstable ISVPs. Through this screen, we did not isolate residues in the core proteins important for these interactions but instead identified several amino acid residues in the μ1 ϕ region that had not been previously associated with ISVP stability. Our second approach focused on targeting specific amino acids residues in the core proteins that vary between type 3 and type 1 serotypes. We generated viruses with chimeric λ1 proteins or with point mutations in σ2. Via this method, we determined specific changes in the core proteins that reduced the stability of ISVPs. Additionally, using these specifically generated mutants, we identified regions λ1 and σ2 that affect events in viral replication distinct from entry. These data highlight the multiple roles for capsid proteins during infection.
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650 4 $a Virology. $3 642304
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653 $a Viral replication
653 $a Viruses
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690 $a 0720
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