Dam and its role in pathogenicity of Salmonella enterica

Centro de Estudios Farmacológicos y Botánicos CEFyBO-CONICET, Departamento de Microbiología, Parasitología e Inmunología, Facultad de Medicina, Universidad de Buenos Aires, Buenos Aires, Argentina.
The Journal of Infection in Developing Countries (Impact Factor: 1.14). 08/2009; 3(7):484-90. DOI: 10.3855/jidc.465
Source: PubMed


Dam methylation is an essential factor involved in the virulence of an increasing number of bacterial pathogens including Salmonella enterica. Lack of Dam methylation causes severe attenuation in animal models. It has been proposed that dysregulation of Dam activity is potentially a general strategy for the generation of vaccines against bacterial pathogens. In this review, we focus our attention on the role of methylation by Dam protein in regulating bacterial gene expression and virulence in Salmonella enterica.

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Available from: Sebastian Sarnacki
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    • "GipA has been shown to be a virulence gene in Salmonella enterica[32]. Analogously, DNA adenine methylase (Dam) is known as an important factor in bacterial virulence [43-45]. The above observations are consistent with the possibility that Fanzor protein could be a methytransferase. "
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    ABSTRACT: Background Bacterial insertion sequences (IS) of IS200/IS605 and IS607 family often encode a transposase (TnpA) and a protein of unknown function, TnpB. Results Here we report two groups of TnpB-like proteins (Fanzor1 and Fanzor2) that are widespread in diverse eukaryotic transposable elements (TEs), and in large double-stranded DNA (dsDNA) viruses infecting eukaryotes. Fanzor and TnpB proteins share the same conserved amino acid motif in their C-terminal half regions: D-X(125, 275)-[TS]-[TS]-X-X-[C4 zinc finger]-X(5,50)-RD, but are highly variable in their N-terminal regions. Fanzor1 proteins are frequently captured by DNA transposons from different superfamilies including Helitron, Mariner, IS4-like, Sola and MuDr. In contrast, Fanzor2 proteins appear only in some IS607-type elements. We also analyze a new Helitron2 group from the Helitron superfamily, which contains elements with hairpin structures on both ends. Non-autonomous Helitron2 elements (CRe-1, 2, 3) in the genome of green alga Chlamydomonas reinhardtii are flanked by target site duplications (TSDs) of variable length (approximately 7 to 19 bp). Conclusions The phylogeny and distribution of the TnpB/Fanzor proteins indicate that they may be disseminated among eukaryotic species by viruses. We hypothesize that TnpB/Fanzor proteins may act as methyltransferases.
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    • "In the context of virulence, methylation has been shown to be an essential PTM in various bacterial pathogens. Using genetic approaches, native methylation has been shown to be required for regulation of transcription and phase variation of outermembrane components (Deitsch et al., 2009), and for maintenance of virulence (Giacomodonato et al., 2009). Methylation of glycolipids has been shown to be essential for Mycobacterium avium virulence in mice (Krzywinska et al., 2005), while methylation of proteins has been shown to alter the antigenicity of the outer-membrane protein OmpB from Rickettsia typhi (Chao et al., 2008), and to alter both the antigenicity of and the host T cell-mediated immune response against the heparin-binding haemagglutinin from Mycobacterium tuberculosis (Parra et al., 2004; Temmerman et al., 2004). "
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