Thomas R et al. (2013) J Med Microbiol "Stenotrophomonas maltophilia: pathogenesis model using Caenorhabditis elegans."

Neela V, Thomas R, Hamat RA

[J Med Microbiol, 2013]

Stenotrophomonas maltophilia plays an important role as an opportunistic pathogen in immunocompromised individuals. Despite its clinical implication, the true knowledge regarding the pathogenicity of these bacteria remains unclear. Various methods have been employed to prove this bacterium to be pathogenic. However, the debate whether S. maltophilia is a true pathogen or a colonizer still remains unanswered as effective killing was not seen in earlier experiments with different animal models of infection (Denton et al., 1998; Adamak et al., 2011; Pompilo et al., 2011). Study by Rouf et al. (2011) on murine lung infection model illustrated that different strains of mice exhibited different outcome for S. maltophilia infection. Strains such as A/J and DBA/2 were permissive for clinical isolates of S. maltophilia and showed higher levels of pro-inflammatory cytokines. In contrast, BALB/c and C57BL/6 strains were non-permissive for S. maltophilia. While Huang et al. (2009) showed nematotoxic activity by environmental S. maltophilia strain against free-living nematode, Panagrellus redivivus, and plant-parasitic nematode, Bursaphelenchus xylophilus.

Petcherski AG et al. (2000) Curr Biol "Mastermind is a putative activator for Notch."

Kimble J, Petcherski AG

[Curr Biol, 2000]

During signaling by the Notch receptor, Notch's intracellular domain is cleaved, moves to the nucleus and associates with a DNA-binding protein of the CSL class (CSL for CBF1, Suppressor of Hairless (Su(H)), LAG-1); as a result, target genes are transcriptionally activated (reviewed in [1,2]). In Caenorhabditis elegans, a glutamine-rich protein called LAG-3 forms a ternary complex with the Notch intracellular domain and LAG-1 and appears to serve as a transcriptional activator that is critical for signaling [3]. Although database searches failed to identify a LAG-3-related protein, we surmised that Notch signaling in other organisms might involve an analogous activity.

Noguez JH et al. (2012) ACS Chem Biol "A novel ascaroside controls the parasitic life cycle of the entomopathogenic nematode Heterorhabditis bacteriophora."

Ragains J, Ciche T, Butcher RA, Conner ES, Zhou Y, Noguez JH

[ACS Chem Biol, 2012]

Entomopathogenic nematodes survive in the soil as stress-resistant infective juveniles that seek out and infect insect hosts. Upon sensing internal host cues, the infective juveniles regurgitate bacterial pathogens from their gut that ultimately kill the host. Inside the host, the nematode develops into a reproductive adult and multiplies until unknown cues trigger the accumulation of infective juveniles. Here, we show that the entomopathogenic nematode Heterorhabditis bacteriophora uses a small-molecule pheromone to control infective juvenile development. The pheromone is structurally related to the dauer pheromone ascarosides that the free-living nematode Caenorhabditis elegans uses to control its development. However, none of the C. elegans ascarosides are effective in H. bacteriophora, suggesting that there is a high degree of species specificity. Our report is the first to show that ascarosides are important regulators of development in a parasitic nematode species. An understanding of chemical signaling in parasitic nematodes may enable the development of chemical tools to control these species.

Singh D et al. (2016) Genesis "Acute heat shock leads to cortical domain internalization and polarity loss in the C. elegans embryo."

Pohl C, Singh D, Odedra D, Lehmann C

[Genesis, 2016]

Many developmental processes are inherently robust due to network organization of the participating factors and functional redundancy. The heterogeneity of the factors involved and their connectivity puts these processes at risk of abrupt system collapse under stress. The polarization of the one-cell C. elegans embryo constitutes such an inherently robust process with functional redundancy. However, how polarization is affected by acute stress has not been thoroughly investigated. Here, we report that heat shock (34C, 1 h) triggers a highly reproducible loss of the anterior and collapse of the posterior polarity domains. Temperature-dependent loss of cortical non-muscle myosin II drastically reduces cortical tension and leads to internalization of large plasma membrane domains including the membrane-associated polarity factor PAR-2. After internalization, plasma membrane vesicles and associated factors cluster around centrosomes and are thereby withdrawn from the polarization process. Transient formation of the posterior polarity domain suggests that microtubule-induced self-organization of this domain is not compromised after heat shock. Hence, our data uncover that the polarization system undergoes a temperature-dependent collapse under acute stress. This article is protected by copyright. All rights reserved.