Molecular mechanisms of bacterial virulence elucidated using a Pseudomonas aeruginosa-Caenorhabditis elegans pathogenesis model.

We reported recently that the human opportunistic pathogen Pseudomonas aeruginosa strain PA14 kills Caenorhabditis elegans and that many P. aeruginosa virulence factors (genes) required for maximum virulence in mouse pathogenicity are also required for maximum killing of C. elegans. Here we report that among eight P. aeruginosa PA14 TnphoA mutants isolated that exhibited reduced killing of C. elegans, at least five also exhibited reduced virulence in mice. Three of the TnphoA mutants corresponded to the known virulence-related genes lasR, gacA, and lemA. Three of the mutants corresponded to known genes (aefA from Escherichia coli, pstP from Azotobacter vinelandii, and mtrR from Neisseria gonorrhoeae) that had not been shown previously to play a role in pathogenesis, and two of the mutants contained TnphoA inserted into novel sequences. These data indicate that the killing of C. elegans by P. aeruginosa can be exploited to identify novel P. aeruginosa virulence factors important for mammalian pathogenesis.

/pdf/pseudomonas-aeruginosa-killing-of-caenorhabditis-elegans-4wj8ke96hj.pdf

Pseudomonas aeruginosa killing of Caenorhabditis elegans used to identify P. aeruginosa virulence factors

hrp genes control the ability of phytopathogenic bacteria to cause disease and to elicit hypersensitive reactions on resistant plants. Genetic and biochemical studies have demonstrated that Hrp proteins are components of Type III secretion systems, regulatory proteins, proteinaceous elicitors of the hypersensitive reaction, and enzymes needed for synthesis of periplasmic glucans. Significantly, Type III secretion systems are involved with the secretion of pathogenicity proteins in bacterial pathogens of animals. The transcriptional activation of a number of bacterial avirulence (avr) genes is controlled by Hrp regulatory proteins, and recent experimental evidence suggests that Avr proteins may be transported by Hrp secretion systems. It has also been hypothesized that pathogenicity and/or virulence gene products exit bacterial phytopathogens via Hrp pathways. Thus, hrp genes may be one of the most important groups of genes found in phytopathogenic bacteria in relationship to pathogenicity and host range.

The role of hrp genes during plant-bacterial interactions.

The hrp gene cluster of Pseudomonas solanacearum GMI1000 strain encodes functions that are essential for pathogenicity on tomato and for the elicitation of the hypersensitive response on tobacco. In this study, we present the nucleotide sequence of one of the hrp genes (hrpB) located at the left-hand end of the cluster and we show that hrpB encodes a positive regulator controlling the expression of hrp genes. hrpB has a coding capacity for a 477-amino-acid polypeptide, which shows significant similarity to several prokaryotic transcriptional activators including the AraC protein of Escherichia coli, the XylS protein of Pseudomonas putida and the VirF protein of Yersinia enterocolitica. The predicted hrpB gene product belongs to a family of bacterial regulators different from the previously described HrpS protein of the hrp gene cluster of Pseudomonas syringae pv. phaseolicola. Genetic evidence demonstrates that the hrpB gene product acts as a positive regulator of the expression in minimal medium of all but one of the putative transcription units of the hrp gene cluster and also controls the expression of genes located outside this cluster. We also show in this paper that the transcription of hrpB is induced in minimal medium and is partly autoregulated.

Evidence that the hrpB gene encodes a positive regulator of pathogenicity genes from Pseudomonas solanacearum.

The capsule is certainly the most obvious virulence factor for Cryptococcus neoformans. The main capsule constituents are glucuronoxylomannans (GXM). Several studies have focused on the structure and chemistry of the GXM component of the capsule, yet little is known about the genetic basis of the capsule construction. Using a monoclonal antibody specific to a sugar epitope, we isolated a capsule-structure mutant strain and cloned by complementation a gene named CAS1 that codes for a putative membrane protein. Although no sequence homology was found with any known protein in the different databases, protein analysis using the PROPSEARCH software classified Cas1p as a putative glycosyltransferase. Cas1p is a well-conserved evolutionary protein, as we identified one orthologue in the human genome, one in the drosophila genome and four in the plant Arabidopsis thaliana genome. Analysis of the capsule structure after CAS1 deletion showed that it is required for GXM O-acetylation.

https://onlinelibrary.wiley.com/doi/pdf/10.1046/j.1365-2958.2001.02651.x

Cas1p is a membrane protein necessary for the O-acetylation of the Cryptococcus neoformans capsular polysaccharide.

One of the chromosomal regions of Pseudomonas syringae pv. syringae encoding pathogenicity factors had been mapped into a 3.9-kilobase-pair fragment in previous studies. Promoter probe analysis indicated the existence of a promoter near one end of the fragment. DNA sequencing of this fragment revealed the existence of a consensus promoter sequence in the region of the promoter activity and two open reading frames (ORFs) downstream. These ORFs, ORF1 and ORF2, encoded putative polypeptides of 40 and 83 kilodaltons, respectively. All ORF1::Tn5 as well as ORF2::Tn5 mutant strains were nonpathogenic on susceptible host bean plants and were unable to elicit hypersensitive reactions on nonhost tobacco plants. The deduced amino acid sequence of the 83-kilodalton polypeptide contained features characteristic of known integral membrane proteins. Fusion of the lacZ gene to ORF2 led to the expression of a hybrid protein inducible in Escherichia coli. The functions of the putative proteins encoded by ORF1 and ORF2 are unknown at present.

Molecular analysis of a pathogenicity locus in Pseudomonas syringae pv. syringae.

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Molecular analysis of a pathogenicity locus in Pseudomonas syringae pv. syringae.