Project description:Insect antennae are important mechanosensory and chemosensory organs. Insect appendages, such as antennae, are encased in a cuticular exoskeleton and are thought to bend only between segments or subsegments where the cuticle is thinner, more flexible, or bent into a fold. There is a growing appreciation of the dominating influence of folds in the mechanical behavior of a structure, and the bending of cricket antennae was considered in this context. Antennae will bend or deflect in response to forces, and the resulting bending behavior will affect the sensory input of the antennae. In some cricket antennae, such as in those of Acheta domesticus, there are a large number (>100) of subsegments (flagellomeres) that vary in their length. We evaluated whether these antennae bend only at the joints between flagellomeres, which has always been assumed but not tested. In addition we questioned whether an antenna undergoes a length change as it bends, which would result from some patterns of joint deformation. Measurements using light microscopy and SEM were conducted on both male and female adult crickets (Acheta domesticus) with bending in four different directions: dorsal, ventral, medial, and lateral. Bending occurred only at the joints between flagellomeres, and antennae shortened a comparable amount during bending, regardless of sex or bending direction. The cuticular folds separating antennal flagellomeres are not very deep, and therefore as an antenna bends, the convex side (in tension) does not have a lot of slack cuticle to "unfold" and does not lengthen during bending. Simultaneously on the other side of the antenna, on the concave side in compression, there is an increasing overlap in the folded cuticle of the joints during bending. Antennal shortening during bending would prevent stretching of antennal nerves and may promote hemolymph exchange between the antenna and head.
Project description:The genome structure of Acheta domesticus mini ambidensovirus, isolated from crickets, resembled that of ambisense densoviruses from Lepidoptera but was 20% smaller. It had the highest (<25%) protein sequence identity with the nonstructural protein 1 (NS1) of Iteravirus and VP of Densovirus members (both with 25% coverage) and smaller (0.2- versus 0.55-kb) Y-shaped inverted terminal repeats.
Project description:The properties of biochar (BC) from crustacean chitin are relatively well understood, while there are few studies on BC from insect chitin. This study presents the characterization and phytotoxic assessment of BC produced from crickets and cricket chitin. Cricket powder (BCCR) and cricket chitin (BCCH) were pyrolyzed at 500 °C and 700 °C. Physicochemical characteristics, N ad-/desorption, FTIR, were examined. SEM images were also performed. Regardless of the pyrolysis temperature, biochars were characterized by a densely “packed” solid surface/monolithic type with a non-porous structure (0.05–0.22 m2/g) and high content of N (9.4–11.8%). BCCHs showed a higher pH (12.2–12.4) compared to BCCR (8.7–10.8). Based on the XRD analysis, BCs were characterized by an amorphous carbon turbostratic structure and a randomly oriented graphitic-like micro-crystallite structure. FTIR spectra of BCs confirmed the presence of various O2 and N-functional groups on the BC surface. BCCHs added to soil at rates from 0.5 to 1.5% significantly reduced the germination of Lepidium sativum. Stimulation of root elongation was also observed in the case of BCCR500 1.0% and BCCR700 1.5%. Thermal degradation of cricket powder and cricket chitin promotes the formation of organic N-containing heterocyclic rings, which lead to the production of N-doped carbons with potential uses in energy storage and the contaminations sorption.
Project description:A novel circular single-stranded DNA (ssDNA) virus, volvovirus, from the house cricket has been described recently. Here, we report the isolation of volvoviruses from Acheta domesticus in Japan and Gryllus assimilis in the United States. These Acheta domesticus volvovirus (AdVVV) isolates have genomes of 2,517 and 2,516 nucleotides (nt) and 4 large open reading frames (ORFs).
Project description:Parvoviruses (family Parvoviridae) are currently defined by a linear monopartite ssDNA genome, T = 1 icosahedral capsids, and distinct structural (VP) and non-structural (NS) protein expression cassettes within their genome. We report the discovery of a parvovirus with a bipartite genome, Acheta domesticus segmented densovirus (AdSDV), isolated from house crickets (Acheta domesticus), in which it is pathogenic. We found that the AdSDV harbors its NS and VP cassettes on two separate genome segments. Its vp segment acquired a phospholipase A2-encoding gene, vpORF3, via inter-subfamily recombination, coding for a non-structural protein. We showed that the AdSDV evolved a highly complex transcription profile in response to its multipartite replication strategy compared to its monopartite ancestors. Our structural and molecular examinations revealed that the AdSDV packages one genome segment per particle. The cryo-EM structures of two empty- and one full-capsid population (3.3, 3.1 and 2.3 Å resolution) reveal a genome packaging mechanism, which involves an elongated C-terminal tail of the VP, "pinning" the ssDNA genome to the capsid interior at the twofold symmetry axis. This mechanism fundamentally differs from the capsid-DNA interactions previously seen in parvoviruses. This study provides new insights on the mechanism behind ssDNA genome segmentation and on the plasticity of parvovirus biology.