Isolation of a Pseudomonas aeruginosa Aspartate Transcarbamoylase Mutant and the Investigation of Its Growth Characteristics, Pyrimidine Biosynthetic Enzyme Activities, and Virulence Factor Production

The pyrimidine biosynthetic pathway is an essential pathway for most organisms. Previous research on the pyrimidine pathway in Pseudomonas aeruginosa (PAO1) has shown that a block in the third step of the pathway resulted in both a requirement for exogenous pyrimidines and decreased ability to produce virulence factors. In this work an organism with a mutation in the second step of the pathway, aspartate transcarbamoylase (ATCase), was created. Assays for pyrimidine intermediates, and virulence factors were performed. Results showed that the production of pigments, haemolysin, and rhamnolipids were significantly decreased from PAO1. Elastase and casein protease production were also moderately decreased. In the Caenorhabditis elegans infection model the nematodes fed the ATCase mutant had increased mortality, as compared to nematodes fed wild type bacteria. These findings lend support to the hypothesis that changes in the pyrimidine biosynthetic pathway contribute to the organism's ability to effect pathogenicity.

Grantor dc:publisher

University of North Texas

Year dc:date

2004

Author dc:creator

• Hammerstein, Heidi Carol

Contributors dc:contributor

• O'Donovan, Gerard A.
• Benjamin, Robert C.
• Bishop, Kathleen L.

• Pyrimidine nucleotides -- Metabolism.
• Pseudomonas aeruginosa.
• Caenorhabditis elegans.
• aspartate transcarbamoylase
• ATCase
• pyrimidine
• virulence factors
• pigments

Statement dc:rights

• Public
• Copyright
• Hammerstein, Heidi Carol
• Copyright is held by the author, unless otherwise noted. All rights reserved.

Language dc:language

English

Identifier

oclc: 58751635
https://digital.library.unt.edu/ark:/67531/metadc4704/
ark: ark:/67531/metadc4704

OAI identifier oai:identifier

info:ark/67531/metadc4704