First record of the Western Grape Leafhopper, Erythroneura elegantula Osborn (Homoptera: Cicadellidae), in Canada

Surveys conducted in the South Okanagan Valley, British Columbia, revealed that a new leafhopper pest of grapes, the western grape leafhopper (WGL), Erythroneura elegantula Osborn, was widespread and often abundant in Vineyards on the east side of the Valley from just north of Penticton south to the United States border. Infestations occurred on drier upland sites where most commercial grape production occurs. The largest populations of up to 40 nymphs per leaf were recorded from commercial Vineyards that had applied reduced rates of the insecticide carbaryl for control of the Virginia creeper leafhopper, E. ziczac Walsh

Leafhopper host plant associations for Anagrus parasitoids (Hymenoptera: Mymaridae) in the Okanagan Valley, British Columbia

Anagrus spp. are important natural regulators of leafhoppers infesting grapes, tree fruits, and other crops in south central British Columbia (BC). Predominantly four species of these egg parasitoids, A. atomus (L.), A. avalae Soyka, A. daanei Triapitsyn, and A. erythroneurae Triapitzyn and Chiappini, were reared from dormant host plants and from summer host plants in the Okanagan Valley. The largest numbers of Anagrus specimens were collected from roses, Rosa spp; blackberry, Rubus spp; apple, Malus domestica; and other members of the rose (Rosaceae) family. Species of mint, family Lamiaceae, were important host plants for several species, with lavender, Lavendula angustifolia, and garden sage, Salvia oficinalis, being both a summer and winter host plant for some species. The most likely leafhopper host on these plants is the mint leafhopper, Eupteryx melissae Curtis. This study contributes to our knowledge of the biology of Anagrus species in south central BC and could contribute to future efforts to preserve or enhance populations of these beneficial insects

Potent and Selective Peptide-based Inhibition of the G Protein Gαq

In contrast to G protein-coupled receptors, for which chemical and peptidic inhibitors have been extensively explored, few compounds are available that directly modulate heterotrimeric G proteins. Active Gα q binds its two major classes of effectors, the phospholipase C (PLC)-β isozymes and Rho guanine nucleotide exchange factors (RhoGEFs) related to Trio, in a strikingly similar fashion: a continuous helix-turn-helix of the effectors engages Gα q within its canonical binding site consisting of a groove formed between switch II and helix α3. This information was exploited to synthesize peptides that bound active Gα q in vitro with affinities similar to full-length effectors and directly competed with effectors for engagement of Gα q A representative peptide was specific for active Gα q because it did not bind inactive Gα q or other classes of active Gα subunits and did not inhibit the activation of PLC-β3 by Gβ 1 γ 2 In contrast, the peptide robustly prevented activation of PLC-β3 or p63RhoGEF by Gα q ; it also prevented G protein-coupled receptor-promoted neuronal depolarization downstream of Gα q in the mouse prefrontal cortex. Moreover, a genetically encoded form of this peptide flanked by fluorescent proteins inhibited Gα q -dependent activation of PLC-β3 at least as effectively as a dominant-negative form of full-length PLC-β3. These attributes suggest that related, cell-penetrating peptides should effectively inhibit active Gα q in cells and that these and genetically encoded sequences may find application as molecular probes, drug leads, and biosensors to monitor the spatiotemporal activation of Gα q in cells