東華大學圖書館 |

Language: English

Help

回圖書館首頁

手機版館藏查詢

Back

Switch To: Labeled | MARC Mode | ISBD

Identification of a region of the he...

Singer, Gregory Philip.

Linked to FindBook

Google Book

Amazon

博客來

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

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Identification of a region of the herpes simplex virus scaffolding protein required for portal interaction, and assembly of portal containing capsids./
Author:	Singer, Gregory Philip.
Description:	124 p.
Notes:	Adviser: Jay Brown.
Contained By:	Dissertation Abstracts International65-10B.
Subject:	Biology, Microbiology. -
Online resource:	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.
LDR:02505nam 2200277 a 45 001 972789
005 20110928
008 110928s2005 eng d
020 $a 9780496089710
035 $a (UnM)AAI3149193
035 $a AAI3149193
040 $a UnM $c UnM
100 1 $a Singer, Gregory Philip. $3 1296759
245 1 0 $a Identification of a region of the herpes simplex virus scaffolding protein required for portal interaction, and assembly of portal containing capsids.
300 $a 124 p.
500 $a Adviser: Jay Brown.
500 $a Source: Dissertation Abstracts International, Volume: 65-10, Section: B, page: 4980.
502 $a Thesis (Ph.D.)--University of Virginia, 2005.
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.
590 $a School code: 0246.
650 4 $a Biology, Microbiology. $3 1017734
650 4 $a Biology, Molecular. $3 1017719
690 $a 0307
690 $a 0410
710 2 0 $a University of Virginia. $3 645578
773 0 $t Dissertation Abstracts International $g 65-10B.
790 $a 0246
790 1 0 $a Brown, Jay, $e advisor
791 $a Ph.D.
792 $a 2005
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3149193