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

Vibrio parahaemolyticus inhibits Rho...

Casselli, Timothy Richard.

Linked to FindBook

Google Book

Amazon

博客來

Vibrio parahaemolyticus inhibits Rho-family GTPase activation via the chromosome 1 type three secreted effector Vp1686.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Vibrio parahaemolyticus inhibits Rho-family GTPase activation via the chromosome 1 type three secreted effector Vp1686./
Author:	Casselli, Timothy Richard.
Published:	Ann Arbor : ProQuest Dissertations & Theses, : 2008,
Description:	192 p.
Notes:	Source: Masters Abstracts International, Volume: 47-03, page: 1499.
Contained By:	Masters Abstracts International47-03.
Subject:	Microbiology. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=MR44577
ISBN:	9780494445778

Vibrio parahaemolyticus inhibits Rho-family GTPase activation via the chromosome 1 type three secreted effector Vp1686.
Casselli, Timothy Richard.

Vibrio parahaemolyticus inhibits Rho-family GTPase activation via the chromosome 1 type three secreted effector Vp1686. - Ann Arbor : ProQuest Dissertations & Theses, 2008 - 192 p.

Source: Masters Abstracts International, Volume: 47-03, page: 1499.

Thesis (M.Sc.)--University of Calgary (Canada), 2008.

Vibrio parahaemolyticus is a leading cause of seafood borne gastroenteritis, however its virulence mechanisms are not well understood. The ability of North American isolates of V. parahaemolyticus to inhibit Rho-family GTPases was examined in cultured HeLa cells and macrophages. Intracellular Rho activation was inhibited in response to external stimuli after infection with clinical and environmental isolates. In vitro activation of Rho, Rac, and Cdc42 isolated from infected cell lysates was also inhibited, indicating that the bacteria were specifically targeting GTPase activation. GTPase inhibition was dependent on translocation of the effector Vp1686 by the chromosome I type three secretion system (T3SS), despite a lack of sequence homology between Vp1686 and known GTPase inhibiting proteins. The ability to inhibit Rho-family GTPases was independent of other virulence factors including the chromosome II T3SS and the haemolytic toxins. The findings reported here contribute to the understanding of virulence mechanisms used by V. parahaemolyticus.

ISBN: 9780494445778Subjects--Topical Terms:

536250
Microbiology.

Vibrio parahaemolyticus inhibits Rho-family GTPase activation via the chromosome 1 type three secreted effector Vp1686.
LDR:01962nmm a2200277 4500 001 2116977
005 20170508094403.5
008 180830s2008 ||||||||||||||||| ||eng d
020 $a 9780494445778
035 $a (MiAaPQ)AAIMR44577
035 $a AAIMR44577
040 $a MiAaPQ $c MiAaPQ
100 1 $a Casselli, Timothy Richard. $3 3278727
245 1 0 $a Vibrio parahaemolyticus inhibits Rho-family GTPase activation via the chromosome 1 type three secreted effector Vp1686.
260 1 $a Ann Arbor : $b ProQuest Dissertations & Theses, $c 2008
300 $a 192 p.
500 $a Source: Masters Abstracts International, Volume: 47-03, page: 1499.
502 $a Thesis (M.Sc.)--University of Calgary (Canada), 2008.
520 $a Vibrio parahaemolyticus is a leading cause of seafood borne gastroenteritis, however its virulence mechanisms are not well understood. The ability of North American isolates of V. parahaemolyticus to inhibit Rho-family GTPases was examined in cultured HeLa cells and macrophages. Intracellular Rho activation was inhibited in response to external stimuli after infection with clinical and environmental isolates. In vitro activation of Rho, Rac, and Cdc42 isolated from infected cell lysates was also inhibited, indicating that the bacteria were specifically targeting GTPase activation. GTPase inhibition was dependent on translocation of the effector Vp1686 by the chromosome I type three secretion system (T3SS), despite a lack of sequence homology between Vp1686 and known GTPase inhibiting proteins. The ability to inhibit Rho-family GTPases was independent of other virulence factors including the chromosome II T3SS and the haemolytic toxins. The findings reported here contribute to the understanding of virulence mechanisms used by V. parahaemolyticus.
590 $a School code: 0026.
650 4 $a Microbiology. $3 536250
650 4 $a Cellular biology. $3 3172791
690 $a 0410
690 $a 0379
710 2 $a University of Calgary (Canada). $3 1017619
773 0 $t Masters Abstracts International $g 47-03.
790 $a 0026
791 $a M.Sc.
792 $a 2008
793 $a English
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=MR44577