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The mechanism of sortase catalyzed c...

Mazmanian, Sarkis Krikor.

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The mechanism of sortase catalyzed cell wall anchoring of surface proteins during gram-positive bacterial infections.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	The mechanism of sortase catalyzed cell wall anchoring of surface proteins during gram-positive bacterial infections./
Author:	Mazmanian, Sarkis Krikor.
Description:	138 p.
Notes:	Chair: Jeffery F. Miller.
Contained By:	Dissertation Abstracts International63-07B.
Subject:	Biology, Cell. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3059578
ISBN:	0493752412

The mechanism of sortase catalyzed cell wall anchoring of surface proteins during gram-positive bacterial infections.
Mazmanian, Sarkis Krikor.

The mechanism of sortase catalyzed cell wall anchoring of surface proteins during gram-positive bacterial infections. - 138 p.

Chair: Jeffery F. Miller.

Thesis (Ph.D.)--University of California, Los Angeles, 2002.

The surfaces of Gram-positive bacteria are decorated with various attached molecules, including carbohydrates, teichoic acids and surface proteins. Though there are several mechanisms for the display of proteins on the microbial exterior, many surface proteins of Gram-positive bacteria are anchored to the cell wall envelope by a transpeptidation mechanism, requiring a C-terminal sorting signal with a conserved LPXTG motif. Sortase, a membrane protein of <italic> Staphylococcus aureus</italic>, cleaves polypeptides between the threonine and the glycine of the LPXTG motif and catalyses the formation of an amide bond between the carboxyl-group of threonine and the amino-group of peptidoglycan cross-bridges. Work presented herein illustrates the isolation and characterization of sortase, the enzymatic machinery that is responsible for the cleavage of sorting signals and cell wall anchoring of surface proteins. Surface proteins are known to perform various biological functions, and most have been demonstrated to be involved during animal infections. The role of sortase in the pathogenesis of Gram-positive bacterial infections is also described. Sortases and surface proteins are conserved in all Gram-positive bacterial genomes. As an extension of these studies the identification and characterization of a second sortase that acts upon a previously unknown sorting signal is also presented. Finally, this study demonstrates an example of how the mechanism of cell wall sorting is utilized by a bacterial pathogen for the essential process of nutrient acquisition.

ISBN: 0493752412Subjects--Topical Terms:

1017686
Biology, Cell.

The mechanism of sortase catalyzed cell wall anchoring of surface proteins during gram-positive bacterial infections.
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100 1 $a Mazmanian, Sarkis Krikor. $3 1251341
245 1 0 $a The mechanism of sortase catalyzed cell wall anchoring of surface proteins during gram-positive bacterial infections.
300 $a 138 p.
500 $a Chair: Jeffery F. Miller.
500 $a Source: Dissertation Abstracts International, Volume: 63-07, Section: B, page: 3143.
502 $a Thesis (Ph.D.)--University of California, Los Angeles, 2002.
520 $a The surfaces of Gram-positive bacteria are decorated with various attached molecules, including carbohydrates, teichoic acids and surface proteins. Though there are several mechanisms for the display of proteins on the microbial exterior, many surface proteins of Gram-positive bacteria are anchored to the cell wall envelope by a transpeptidation mechanism, requiring a C-terminal sorting signal with a conserved LPXTG motif. Sortase, a membrane protein of <italic> Staphylococcus aureus</italic>, cleaves polypeptides between the threonine and the glycine of the LPXTG motif and catalyses the formation of an amide bond between the carboxyl-group of threonine and the amino-group of peptidoglycan cross-bridges. Work presented herein illustrates the isolation and characterization of sortase, the enzymatic machinery that is responsible for the cleavage of sorting signals and cell wall anchoring of surface proteins. Surface proteins are known to perform various biological functions, and most have been demonstrated to be involved during animal infections. The role of sortase in the pathogenesis of Gram-positive bacterial infections is also described. Sortases and surface proteins are conserved in all Gram-positive bacterial genomes. As an extension of these studies the identification and characterization of a second sortase that acts upon a previously unknown sorting signal is also presented. Finally, this study demonstrates an example of how the mechanism of cell wall sorting is utilized by a bacterial pathogen for the essential process of nutrient acquisition.
590 $a School code: 0031.
650 4 $a Biology, Cell. $3 1017686
650 4 $a Biology, Microbiology. $3 1017734
690 $a 0379
690 $a 0410
710 2 0 $a University of California, Los Angeles. $3 626622
773 0 $t Dissertation Abstracts International $g 63-07B.
790 $a 0031
790 1 0 $a Miller, Jeffery F., $e advisor
791 $a Ph.D.
792 $a 2002
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3059578