Open AccessDeletion of the gene encoding the glycolytic enzyme triosephosphate isomerase ( tpi ) alters morphology of Salmonella enterica serovar Typhimurium and decreases fitness in mice
Author(s) -
Paterson Gavin K.,
Cone Danielle B.,
Northen Helen,
Peters Sarah E.,
Maskell Duncan J.
Publication year - 2009
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2009.01553.x
Subject(s) - salmonella enterica , triosephosphate isomerase , biology , mutant , microbiology and biotechnology , salmonella , pathogen , enzyme , enterobacteriaceae , glycolysis , gene , bacteria , escherichia coli , genetics , biochemistry
The glycolytic enzyme triosephosphate isomerase ( tpi ) (EC 5.3.1.1) plays a key role in central carbon metabolism yet few studies have characterized isogenic bacterial mutants lacking this enzyme and none have examined its role in the in vivo fitness of a bacterial pathogen. Here we have deleted tpiA in Salmonella enterica serovar Typhimurium and found that the mutant had an altered morphology, displaying an elongated shape compared with the wild type. In a mouse model of typhoid fever the tpiA mutant was attenuated for growth as assessed by bacterial counts in the livers and spleens of infected mice. However, this attenuation was not deemed sufficient for consideration of a tpiA mutant as a live attenuated vaccine strain. These phenotypes were complemented by provision of tpiA on pBR322. We therefore provide the first demonstration that tpiA is required for full in vivo fitness of a bacterial pathogen, and that it has a discernable impact on cell morphology.