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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 Inra
Velge, P.; Herler, M.; Johansson, J.; Roche, S.; Témoin, S.; Fedorov, A. A.; Gracieux, P.; Almo, S. C.; Goebel, W.; Cossart, P..
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 EGDΔprfA strain did not restore the haemolytic and phosphatidylcholine phospholipase C activities, in contrast to the wild-type prfA gene. The substitution of the lysine at position 220 occurred in the helix αH. However, the data showed that the PrfAK220T protein is dimerized just as well as its wild-type counterpart, but does not bind to PrfA boxes....
Tipo: Journal Article Palavras-chave: LISTERIA MONOCYTOGENES; PROTEINE; FACTEUR DE VIRULENCE; BACTERIE PATHOGENE; ADN; SEQUENCE NUCLEOTIDIQUE; REGULATION; TRANSCRIPTION; VIRULENCE; EXPRESSION DES GENES; ACIDE AMINE; MUTATION; RT-PCR; ELECTROPHORESE; ENZYME; ARN POLYMERASE.
Ano: 2007 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2009c1895b3c&uri=/notices/prodinra1/2009/11/
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