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Structure and function studies of th...

Odegard, Amy L.

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Structure and function studies of the reovirus membrane penetration protein mu1.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Structure and function studies of the reovirus membrane penetration protein mu1./
作者:	Odegard, Amy L.
面頁冊數:	210 p.
附註:	Source: Dissertation Abstracts International, Volume: 65-04, Section: B, page: 1850.
Contained By:	Dissertation Abstracts International65-04B.
標題:	Chemistry, Biochemistry. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3128031
ISBN:	0496752944

Structure and function studies of the reovirus membrane penetration protein mu1.
Odegard, Amy L.

Structure and function studies of the reovirus membrane penetration protein mu1. - 210 p.

Source: Dissertation Abstracts International, Volume: 65-04, Section: B, page: 1850.

Thesis (Ph.D.)--The University of Wisconsin - Madison, 2004.

In general, RNA viruses must cross the cellular membrane during infection to gain access to the host cell cytoplasm, where viral replication takes place. Since nonenveloped viruses lack a viral membrane, they must traverse the lipid bilayer by a means other than fusion. Studies of mammalian reovirus entry provide a model for membrane penetration that inapplicable to diverse families of nonenveloped viruses. The viral outer capsid protein mu1 is known to play a key role in reovirus entry and membrane penetration. Studies described in this dissertation examine the importance of specific structural features of mu1 as they relate to reovirus entry.

ISBN: 0496752944Subjects--Topical Terms:

1017722
Chemistry, Biochemistry.

Structure and function studies of the reovirus membrane penetration protein mu1.
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245 1 0 $a Structure and function studies of the reovirus membrane penetration protein mu1.
300 $a 210 p.
500 $a Source: Dissertation Abstracts International, Volume: 65-04, Section: B, page: 1850.
500 $a Supervisor: Max L. Nibert.
502 $a Thesis (Ph.D.)--The University of Wisconsin - Madison, 2004.
520 $a In general, RNA viruses must cross the cellular membrane during infection to gain access to the host cell cytoplasm, where viral replication takes place. Since nonenveloped viruses lack a viral membrane, they must traverse the lipid bilayer by a means other than fusion. Studies of mammalian reovirus entry provide a model for membrane penetration that inapplicable to diverse families of nonenveloped viruses. The viral outer capsid protein mu1 is known to play a key role in reovirus entry and membrane penetration. Studies described in this dissertation examine the importance of specific structural features of mu1 as they relate to reovirus entry.
520 $a In the first set of studies, the importance of a mu1-mu1 intermolecular disulfide bond (ds) on the surface of the reovirus capsid was addressed. This ds bond was localized to mu1 residue Cys679 and predicted to form between mu1 subunits from adjacent trimers. Recoated particles containing a non-ds-bonding mutant of mu1 (Cys679 substituted by serine) were generated, indicating that the ds bond is not essential for outer capsid assembly. In addition, infectivity experiments revealed the ds bond was not required for productive infection. While these studies suggest that ds formation is dispensable, it remains possible that once formed, the ds bond must be reduced to permit mu1 entry-related conformational changes and uncoating.
520 $a In a second set of studies, the importance of mu1 autoproteolytic cleavage was addressed. This cleavage generates two fragments, a large carboxy-terminal fragment, mu1C, and a small hydrophobic amino-terminal fragment, mu1N. Recoated particles containing a cleavage-defective mu1 mutant were generated, indicating this cleavage is not required for outer capsid assembly. These cleavage-defective recoated particles were poorly infectious and specifically blocked at the membrane penetration step during entry. Additional experiments revealed that the myristoylated mu1N fragment is normally released from reovirus particles during entry-related uncoating. Therefore, it is hypothesized that released mu1N may play a role in membrane disruption, explaining the infectivity and membrane penetration defect of cleavage-defective recoated cores. Release of a small hydrophobic peptide following autoproteolytic cleavage has been demonstrated for several other nonenveloped animal viruses, suggesting these viruses may share related membrane penetration mechanisms.
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650 4 $a Biology, Microbiology. $3 1017734
650 4 $a Biology, Molecular. $3 1017719
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710 2 0 $a The University of Wisconsin - Madison. $3 626640
773 0 $t Dissertation Abstracts International $g 65-04B.
790 1 0 $a Nibert, Max L., $e advisor
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791 $a Ph.D.
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