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Identification of a region of the he...

Singer, Gregory Philip.

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Identification of a region of the herpes simplex virus scaffolding protein required for portal interaction, and assembly of portal containing capsids.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Identification of a region of the herpes simplex virus scaffolding protein required for portal interaction, and assembly of portal containing capsids./
作者:	Singer, Gregory Philip.
面頁冊數:	124 p.
附註:	Adviser: Jay Brown.
Contained By:	Dissertation Abstracts International65-10B.
標題:	Biology, Microbiology. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3149193
ISBN:	9780496089710

Identification of a region of the herpes simplex virus scaffolding protein required for portal interaction, and assembly of portal containing capsids.
Singer, Gregory Philip.

Identification of a region of the herpes simplex virus scaffolding protein required for portal interaction, and assembly of portal containing capsids. - 124 p.

Adviser: Jay Brown.

Thesis (Ph.D.)--University of Virginia, 2005.

The herpes simplex virus (HSV-1) capsid is a hard, protective shell that acts as a container for the genetic material of the virus. After assembly of the capsid, the viral DNA is translocated into the capsid interior through a channel formed by the portal. The portal is composed of a dodecamer of UL6 molecules, which form a ring-like structure found only at a single vertex within the icosahedron. Formation of portal containing capsids minimally requires the four structural proteins (VP5, VP19C, VP23 and UL6) and a scaffolding protein (UL26.5). Recently an interaction between UL26.5 and the portal has been identified, suggesting the scaffold is responsible for recognizing the portal and incorporating it into the capsid shell. The aim of this study was to identify regions within the UL26.5 that mediate its interaction with the portal. A specific region was identified by mutational analysis. Deletion of scaffold as 143--151 was found to be sufficient to completely abrogate formation of the scaffold-portal complex as assayed in vitro. Amino acids 143--151 contain the sequence YYPGE, which is highly conserved among alphaherpesviruses. Although it did not bind to the portal, the Delta143--151 mutant was found to retain the ability to support assembly of morphologically normal capsids in vitro. These capsids, however, did not contain the portal. The results suggest assembly of portal-containing capsids requires the formation of a scaffold-portal complex in which intermolecular contact is mediated by scaffold amino acids in the 143--151 region.

ISBN: 9780496089710Subjects--Topical Terms:

1017734
Biology, Microbiology.

Identification of a region of the herpes simplex virus scaffolding protein required for portal interaction, and assembly of portal containing capsids.
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520 $a The herpes simplex virus (HSV-1) capsid is a hard, protective shell that acts as a container for the genetic material of the virus. After assembly of the capsid, the viral DNA is translocated into the capsid interior through a channel formed by the portal. The portal is composed of a dodecamer of UL6 molecules, which form a ring-like structure found only at a single vertex within the icosahedron. Formation of portal containing capsids minimally requires the four structural proteins (VP5, VP19C, VP23 and UL6) and a scaffolding protein (UL26.5). Recently an interaction between UL26.5 and the portal has been identified, suggesting the scaffold is responsible for recognizing the portal and incorporating it into the capsid shell. The aim of this study was to identify regions within the UL26.5 that mediate its interaction with the portal. A specific region was identified by mutational analysis. Deletion of scaffold as 143--151 was found to be sufficient to completely abrogate formation of the scaffold-portal complex as assayed in vitro. Amino acids 143--151 contain the sequence YYPGE, which is highly conserved among alphaherpesviruses. Although it did not bind to the portal, the Delta143--151 mutant was found to retain the ability to support assembly of morphologically normal capsids in vitro. These capsids, however, did not contain the portal. The results suggest assembly of portal-containing capsids requires the formation of a scaffold-portal complex in which intermolecular contact is mediated by scaffold amino acids in the 143--151 region.
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