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The effects of serine and acetate me...

Anfora, Andrew Thomas.

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The effects of serine and acetate metabolism on the ability of Escherichia coli CFT073 to colonize the murine urinary tract.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	The effects of serine and acetate metabolism on the ability of Escherichia coli CFT073 to colonize the murine urinary tract./
Author:	Anfora, Andrew Thomas.
Description:	169 p.
Notes:	Adviser: Rodney A. Welch.
Contained By:	Dissertation Abstracts International68-08B.
Subject:	Biology, Microbiology. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3278810
ISBN:	9780549195108

The effects of serine and acetate metabolism on the ability of Escherichia coli CFT073 to colonize the murine urinary tract.
Anfora, Andrew Thomas.

The effects of serine and acetate metabolism on the ability of Escherichia coli CFT073 to colonize the murine urinary tract. - 169 p.

Adviser: Rodney A. Welch.

Thesis (Ph.D.)--The University of Wisconsin - Madison, 2007.

Uropathogenic Escherichia coli are the causative agents of the majority of community acquired urinary tract infections. D-serine is an amino acid found in mammalian urine present at 3-120 [uglml in human urine. E. coli are able to respond to the presence of D-serine in both human and murine urine. D-serine is bacteriostatic to E. coli unable to express the D-serine deaminase protein, DsdA, grown in minimal media amended with 50 pg/ml D-serine. E. coli CFT073 dsdA is severely impaired in the ability to grow in human urine compared to wild-type CFT073. Counterintuitively, E. coli CFF073 dsdA outcompetes wild-type in co-infection of the murine model or urinary tract infection. CFT073 dsdA mutants recovered from the urine of infected mice show an up-regulation of the virulence associated traits coding for adhesins and toxins by an unknown mechanism. In order to address the cause of the up-regulation of the virulence-associated traits, we monitored carbon metabolism in E. coli CFT073. We first examined how D-serine enters the bacterial cell by characterizing the two D-serine inner membrane permeases, DsdX and CycA. Next we demonstrate that the increased colonization seen with E. coli CFT073 dsdA requires the intracellular accumulation of D-serine but not of L-serine and that accumulation of both serine enantiomers is detrimental to colonization of the urinary tract. The detrimental effects following accumulation of both serine enantiomers may be due to loss of catabolic by-products of pyruvate catabolism, especially acetyl phosphate. We demonstrate that E. coli CFF073 is better adapted to growth on acetogenic substrates than is E. coli K-12 isolate MG1655. Finally, we demonstrate that the ability to efficiently catabolize secreted acetate is not important for colonization of the murine urinary tract, but loss of the genes responsible for regulating the intracellular acetyl phosphate pool, ackA and pta, decreases fitness in the murine urinary tract. We speculate that the phenotypes are tied to the ability to respond to membrane stress.

ISBN: 9780549195108Subjects--Topical Terms:

1017734
Biology, Microbiology.

The effects of serine and acetate metabolism on the ability of Escherichia coli CFT073 to colonize the murine urinary tract.
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020 $a 9780549195108
035 $a (UMI)AAI3278810
035 $a AAI3278810
040 $a UMI $c UMI
100 1 $a Anfora, Andrew Thomas. $3 1270481
245 1 4 $a The effects of serine and acetate metabolism on the ability of Escherichia coli CFT073 to colonize the murine urinary tract.
300 $a 169 p.
500 $a Adviser: Rodney A. Welch.
500 $a Source: Dissertation Abstracts International, Volume: 68-08, Section: B, page: 4984.
502 $a Thesis (Ph.D.)--The University of Wisconsin - Madison, 2007.
520 $a Uropathogenic Escherichia coli are the causative agents of the majority of community acquired urinary tract infections. D-serine is an amino acid found in mammalian urine present at 3-120 [uglml in human urine. E. coli are able to respond to the presence of D-serine in both human and murine urine. D-serine is bacteriostatic to E. coli unable to express the D-serine deaminase protein, DsdA, grown in minimal media amended with 50 pg/ml D-serine. E. coli CFT073 dsdA is severely impaired in the ability to grow in human urine compared to wild-type CFT073. Counterintuitively, E. coli CFF073 dsdA outcompetes wild-type in co-infection of the murine model or urinary tract infection. CFT073 dsdA mutants recovered from the urine of infected mice show an up-regulation of the virulence associated traits coding for adhesins and toxins by an unknown mechanism. In order to address the cause of the up-regulation of the virulence-associated traits, we monitored carbon metabolism in E. coli CFT073. We first examined how D-serine enters the bacterial cell by characterizing the two D-serine inner membrane permeases, DsdX and CycA. Next we demonstrate that the increased colonization seen with E. coli CFT073 dsdA requires the intracellular accumulation of D-serine but not of L-serine and that accumulation of both serine enantiomers is detrimental to colonization of the urinary tract. The detrimental effects following accumulation of both serine enantiomers may be due to loss of catabolic by-products of pyruvate catabolism, especially acetyl phosphate. We demonstrate that E. coli CFF073 is better adapted to growth on acetogenic substrates than is E. coli K-12 isolate MG1655. Finally, we demonstrate that the ability to efficiently catabolize secreted acetate is not important for colonization of the murine urinary tract, but loss of the genes responsible for regulating the intracellular acetyl phosphate pool, ackA and pta, decreases fitness in the murine urinary tract. We speculate that the phenotypes are tied to the ability to respond to membrane stress.
590 $a School code: 0262.
650 4 $a Biology, Microbiology. $3 1017734
690 $a 0410
710 2 $a The University of Wisconsin - Madison. $3 626640
773 0 $t Dissertation Abstracts International $g 68-08B.
790 $a 0262
790 1 0 $a Welch, Rodney A., $e advisor
791 $a Ph.D.
792 $a 2007
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3278810