Bacterial Factors Required for Transmission of Streptococcus pneumoniae in Mammalian Hosts

1. Download : Download high-res image (224KB)
2. Download : Download full-size image

     

Diet quality mitigates intraspecific larval competition in Drosophila suzukii

The invasive frugivore Drosophila suzukii (Matsumura) (Diptera: Drosophilidae) utilizes a wide range of host plants and damages important fruit crops, including blueberries, cherries, blackberries, raspberries, and strawberries. Field infestations of D. suzukii often exceed one larva per berry, suggesting that intraspecific competition may frequently occur. Because dietary resources are also likely to vary across the host range of D. suzukii, we designed a laboratory assay to measure larval performance across diets of varying quality: a standard artificial diet, a fruit‐based medium, a low‐protein, and a low‐carbohydrate diet. We manipulated egg density across these diets to provide increasing levels of competition and measured larval performance by observing survival to pupation and adulthood, and development times for both life stages. Although increasing density generally negatively impacted D. suzukii performance across diets, the magnitude of these impacts varied by diet type. Drosophila suzukii performance was generally similar in fruit and standard diets, although larval development was more rapid in fruit diets at lower densities. Even at low densities (5 or 10 eggs per arena), survival was reduced and development time increased in low‐protein diets relative to standard and fruit diets. At the two highest larval densities (20 or 40 eggs per arena), survivorship was reduced in low‐carbohydrate diets as compared to standard and fruit diets. There is evidence that larvae compensated in both low‐quality diets by extending development time, which could have consequences for population dynamics. Population models for use in D. suzukii management may need to account for both host nutritional quality and relative competition to accurately predict turnover and geographic expansion.     

Plant choice,herbivory and weight gain of wood crickets under the risk of predation

Predators can indirectly reduce herbivory by killing herbivores. In addition, predation risk can influence the feeding rate and feeding location of herbivores. Herbivores are expected to avoid plants currently occupied by a predator. Consequently, less herbivory is expected on plants bearing fresh predator cues. We examined whether wood crickets, Nemobius sylvestris Bosc (Orthoptera: Gryllidae), avoided plants bearing the chemical cues of nursery web spiders, Pisaura mirabilis Clerck (Araneae: Pisauridae), or red wood ants, Formica rufa L. (Hymenoptera: Formicidae). We conducted a series of behavioural experiments, in which crickets had the choice between a plant with spider or ant cues vs. a control plant, a plant with spider cues vs. a plant with ant cues, or two control plants. For all plants, we quantified leaf damage and the position and weight change in the crickets. Crickets avoided plants with spider cues. In contrast, ant cues did not significantly deter crickets. The herbivory pattern among the plants reflected the plant choice of the crickets. However, net herbivory was not affected by the presence of predator cues. Thus, our results suggest that spider cues affect feeding location rather than the total amount of herbivory.     

HtrC Is Involved in Proteolysis of YpeB during Germination of Bacillus anthracis and Bacillus subtilis Spores

Bacterial endospores can remain dormant for decades yet can respond to nutrients, germinate, and resume growth within minutes. An essential step in the germination process is degradation of the spore cortex peptidoglycan wall, and the SleB protein in Bacillus species plays a key role in this process. Stable incorporation of SleB into the spore requires the YpeB protein, and some evidence suggests that the two proteins interact within the dormant spore. Early during germination, YpeB is proteolytically processed to a stable fragment. In this work, the primary sites of YpeB cleavage were identified in Bacillus anthracis, and it was shown that the stable products are comprised of the C-terminal domain of YpeB. Modification of the predominant YpeB cleavage sites reduced proteolysis, but cleavage at other sites still resulted in loss of full-length YpeB. A B. anthracis strain lacking the HtrC protease did not generate the same stable YpeB products. In B. anthracis and Bacillus subtilis htrC mutants, YpeB was partially stabilized during germination but was still degraded at a reduced rate by other, unidentified proteases. Purified HtrC cleaved YpeB to a fragment similar to that observed in vivo, and this cleavage was stimulated by Mn²⁺ or Ca²⁺ ions. A lack of HtrC did not stabilize YpeB or SleB during spore formation in the absence of the partner protein, indicating other proteases are involved in their degradation during sporulation.     

LLY-507, a Cell-active,Potent, and Selective Inhibitor of Protein-lysine Methyltransferase SMYD2

SMYD2 is a lysine methyltransferase that catalyzes the monomethylation of several protein substrates including p53. SMYD2 is overexpressed in a significant percentage of esophageal squamous primary carcinomas, and that overexpression correlates with poor patient survival. However, the mechanism(s) by which SMYD2 promotes oncogenesis is not understood. A small molecule probe for SMYD2 would allow for the pharmacological dissection of this biology. In this report, we disclose LLY-507, a cell-active, potent small molecule inhibitor of SMYD2. LLY-507 is >100-fold selective for SMYD2 over a broad range of methyltransferase and non-methyltransferase targets. A 1.63-Å resolution crystal structure of SMYD2 in complex with LLY-507 shows the inhibitor binding in the substrate peptide binding pocket. LLY-507 is active in cells as measured by reduction of SMYD2-induced monomethylation of p53 Lys³⁷⁰ at submicromolar concentrations. We used LLY-507 to further test other potential roles of SMYD2. Mass spectrometry-based proteomics showed that cellular global histone methylation levels were not significantly affected by SMYD2 inhibition with LLY-507, and subcellular fractionation studies indicate that SMYD2 is primarily cytoplasmic, suggesting that SMYD2 targets a very small subset of histones at specific chromatin loci and/or non-histone substrates. Breast and liver cancers were identified through in silico data mining as tumor types that display amplification and/or overexpression of SMYD2. LLY-507 inhibited the proliferation of several esophageal, liver, and breast cancer cell lines in a dose-dependent manner. These findings suggest that LLY-507 serves as a valuable chemical probe to aid in the dissection of SMYD2 function in cancer and other biological processes.