東華大學圖書館 |

語系: 繁體中文

說明(常見問題)

回圖書館首頁

手機版館藏查詢

登入

回首頁

切換: 標籤 | MARC模式 | ISBD

DNA packaging, capsid assembly and e...

Dasgupta, Anindya.

FindBook

Google Book

Amazon

博客來

DNA packaging, capsid assembly and egress of HSV-1: A biochemical study.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	DNA packaging, capsid assembly and egress of HSV-1: A biochemical study./
作者:	Dasgupta, Anindya.
面頁冊數:	125 p.
附註:	Adviser: Duncan W. Wilson.
Contained By:	Dissertation Abstracts International63-01B.
標題:	Biology, Molecular. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3041000
ISBN:	0493543198

DNA packaging, capsid assembly and egress of HSV-1: A biochemical study.
Dasgupta, Anindya.

DNA packaging, capsid assembly and egress of HSV-1: A biochemical study. - 125 p.

Adviser: Duncan W. Wilson.

Thesis (Ph.D.)--Yeshiva University, 2002.

Herpes Simplex Virus Type 1 is a causative agent for a number of diseases in humans. The assembly process initiates in the nuclei of infected cells, where viral DNA replication and capsid assembly takes place and viral genomes are packaged into capsids which are then thought to bud into the inner nuclear membrane, generating enveloped particles in the perinuclear space. These particles then exit the nucleus and traffic out of the cell.

ISBN: 0493543198Subjects--Topical Terms:

1017719
Biology, Molecular.

DNA packaging, capsid assembly and egress of HSV-1: A biochemical study.
LDR:03253nam 2200325 a 45 001 935985
005 20110510
008 110510s2002 eng d
020 $a 0493543198
035 $a (UnM)AAI3041000
035 $a AAI3041000
040 $a UnM $c UnM
100 1 $a Dasgupta, Anindya. $3 1259685
245 1 0 $a DNA packaging, capsid assembly and egress of HSV-1: A biochemical study.
300 $a 125 p.
500 $a Adviser: Duncan W. Wilson.
500 $a Source: Dissertation Abstracts International, Volume: 63-01, Section: B, page: 0083.
502 $a Thesis (Ph.D.)--Yeshiva University, 2002.
520 $a Herpes Simplex Virus Type 1 is a causative agent for a number of diseases in humans. The assembly process initiates in the nuclei of infected cells, where viral DNA replication and capsid assembly takes place and viral genomes are packaged into capsids which are then thought to bud into the inner nuclear membrane, generating enveloped particles in the perinuclear space. These particles then exit the nucleus and traffic out of the cell.
520 $a Using a reversible temperature sensitive mutant <italic>ts</italic> Prot.A, we have been able to synchronize viral assembly. We have also developed rapid biochemical assays to measure DNA packaging and envelopment of HSV-1. These assays were based on the hypothesis that the packaged genomes would be resistant to DnaseI treatment, compared to unpackaged DNA. Using the synchronized assembly system and the assays we developed, we have been able to determine the kinetics of DNA packaging and envelopment of HSV-1 in infected cells. We also observed that in the absence of ATP, no infectious viral particles are produced and that DNA packaging and capsid assembly are ATP dependent processes.
520 $a Once the packaged capsids exit the nucleus, the route that it takes to exit the cell is a contentious issue. One view, the single envelopment model, is that the perinuclear virions traffic out of the cell <italic>via</italic> the classical secretory pathway. An alternative view is that the initial envelope the virions acquired from the inner nuclear membrane fuses with the outer nuclear membrane to release naked capsids into the cytoplasm which then bud into an organelle such as the Golgi, Trans Golgi network (TGN) or endosomes, and acquire their final envelope.
520 $a To distinguish between the two models, we used the fungal metabolite Brefeldin A (BFA). BFA is an agent that blocks endoplasmic reticulum (ER) to Golgi trafficking. If the first model is true, then there should be an increase in naked cytoplasmic capsids.
520 $a Surprisingly, however, we observed none of the predicted results. Under our conditions, packaged capsids become trapped within the nucleoplasm and fail to bud into the perinuclear space and traffic into the cytoplasm. We conclude that the immediate effect of BFA upon the assembly pathway of HSV is to block capsid envelopment at the inner nuclear membrane.
590 $a School code: 0266.
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Chemistry, Biochemistry. $3 1017722
690 $a 0307
690 $a 0487
710 2 0 $a Yeshiva University. $3 1017732
773 0 $t Dissertation Abstracts International $g 63-01B.
790 $a 0266
790 1 0 $a Wilson, Duncan W., $e advisor
791 $a Ph.D.
792 $a 2002
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3041000