A naturally occurring mutation K220T in the pleiotropic activator PrfA of Listeria monocytogenes results in a loss of virulence due to decreasing DNA-binding affinity.

@article{Velge2007ANO,
  title={A naturally occurring mutation K220T in the pleiotropic activator PrfA of Listeria monocytogenes results in a loss of virulence due to decreasing DNA-binding affinity.},
  author={Philippe Velge and Michael Herler and J{\"o}rgen Johansson and Sylvie Marie Roche and St{\'e}phanie T{\'e}moin and Al. A. Fedorov and Patrice Gracieux and Steven C. Almo and W. Goebel and Pascale Cossart},
  journal={Microbiology},
  year={2007},
  volume={153 Pt 4},
  pages={
          995-1005
        }
}
The sequencing of prfA, encoding the transcriptional regulator of virulence genes, in 26 low-virulence field Listeria monocytogenes strains showed that eight strains exhibited the same single amino-acid substitution: PrfAK220T. These strains exhibited no expression of PrfA-regulated proteins and thus no virulence. This substitution inactivated PrfA, since expression of the PrfAK220T mutant gene in an EGDDeltaprfA strain did not restore the haemolytic and phosphatidylcholine phospholipase C… CONTINUE READING

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