PLoS ONE · 2010 · 95 citations · 41 references
Life SciencesMicrobiologyMolecular BiologyGene ExpressionHost-pathogen InteractionsMicrobial PathogenesisBacterial Gene RegulationBacterial PathogenesisBacterial Virulence FactorsMicrobial Virulence FactorsPathogen Virulence FactorsVirulence Gene RegulationCarotenoid ProductionDifferential Transcript ExpressionPathogenicity Factor ExpressionPigmentsRna Binding Protein RegulationRna-binding Protein InteractionsRna-protein BindingStress Response In Pathogenesis
The Hfq protein is reported to be an RNA chaperone, which is involved in the stress response and the virulence of several pathogens. In E. coli, Hfq can mediate the interaction between some sRNAs and their target mRNAs. But it is controversial whether Hfq plays an important role in S. aureus. In this study, we found that the deletion of hfq gene in S. aureus 8325-4 can increase the surface carotenoid pigments. The hfq mutant was more resistant to oxidative stress but the pathogenicity of the mutant was reduced. We reveal that the Hfq protein can be detected only in some S. aureus strains. Using microarray and qRT-PCR, we identified 116 genes in the hfq mutant which had differential expression from the wild type, most of which are related to the phenotype and virulence of S. aureus. Among the 116 genes, 49 mRNAs can specifically bind Hfq protein, which indicates that Hfq also acts as an RNA binding protein in S. aureus. Our data suggest that Hfq protein of S. aureus is a multifunctional regulator involved in stress and virulence.
41
The toxic shock syndrome exotoxin structural gene is not detectably transmitted by a prophage
Barry N. Kreiswirth, Sven Löfdahl, M J Betley et al. · Nature · 1983 · 1.3K citations
George Y. Liu, Anthony Essex, John T. Buchanan et al. · The Journal of Experimental Medicine · 2005 · 755 citations · Full text