22
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      Effect of Venom from the Jellyfish Nemopilema nomurai on the Silkworm Bombyx mori L

      research-article

      Read this article at

          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          The silkworm Bombyx mori L. ( B. mori) has a significant impact on the economy by producing more than 80% of the globally produced raw silk. The exposure of silkworm to pesticides may cause adverse effects on B. mori, such as a reduction in the production and quality of silk. This study aims to assay the effect of venom from the jellyfish Nemopilema nomurai on growth, cuticle and acetylcholinesterase (AChE) activity of the silkworm B. mori by the leaf dipping method. The experimental results revealed that the four samples caused neither antifeeding nor a lethal effect on B. mori. The sample SFV inhibited B. mori growth after 6 days of treatment in a dose-dependent manner. The samples SFV, DSFV and Fr-1 inhibited the precipitation and synthesis of chitin in the cuticle after 12 and 14 days of treatment. In the case of the four samples, the AChE was significantly improved after 14 days of treatment.

          Related collections

          Most cited references45

          • Record: found
          • Abstract: found
          • Article: not found

          Chitin synthesis and inhibition: a revisit.

          Chitin is an abundant biologically important aminopolysaccharide composed of N-acetyl-D-glucosamine units. Individual polymers, which are synthesized intracellularly by chitin synthase (CS), a membrane-bound glycosyl transferase, are translocated across the plasma membrane and coalesce to form rigid crystallites. These crystallites, inter alia, are integral parts of septa and cell walls in yeast and filamentous fungi, respectively, and of cuticles in invertebrates, notably crustaceans and insects. Despite decades of intensive research, many events associated with the complexity of chitin formation and deposition are still obscure, or only partially understood. The list includes the hormonal control of CS at the transcriptional and translational levels as well as the post-translational CS packaging; trafficking and guidance of CS clusters to proper sites in the cells and their intricate insertion into the plasma membranes; activation of the catalytic step and its control or modulation; and translocation of chitin chains across cell membranes, their orientation, fibrillogenesis and association with other extracellular structural components such as polysaccharides (fungi) and cuticular proteins (insects). Also the precise biochemical lesions inflicted by CS inhibitors, such as the acylurea insect growth regulators, are largely unclear. The recent isolation and sequencing of insect CS genes should help in elucidating various aspects of chitin biochemistry and inhibition. In particular, the large number of transmembrane segments, characteristic of the insect CS, are speculated to be involved in chitin translocation and are expected to shed light on the mode of action of acylurea insecticides.
            • Record: found
            • Abstract: found
            • Article: not found

            Were arachnids the first to use combinatorial peptide libraries?

            Spiders, scorpions, and cone snails are remarkable for the extent and diversity of gene-encoded peptide neurotoxins that are expressed in their venom glands. These toxins are produced in the form of structurally constrained combinatorial peptide libraries in which there is hypermutation of essentially all residues in the mature-toxin sequence with the exception of a handful of strictly conserved cysteines that direct the three-dimensional fold of the toxin. This gene-based combinatorial peptide library strategy appears to have been first implemented by arachnids almost 400 million years ago, long before cone snails evolved a similar mechanism for generating peptide diversity.
              • Record: found
              • Abstract: found
              • Article: not found

              Involvement of chitin in exoskeleton morphogenesis in Drosophila melanogaster.

              Exoskeletons stabilize cell, tissue, and body morphology in many living organisms including fungi, plants, and arthropods. In insects, the exoskeleton, the cuticle, is produced by epidermal cells as a protein extracellular matrix containing lipids and the polysaccharide chitin, and its formation requires coordinated synthesis, distribution, and modification of these components. Eventually, the stepwise secretion and sorting of the cuticle material results in a layered structure comprising the envelope, the proteinaceous epicuticle, and the chitinous procuticle. To study the role of chitin during cuticle development, we analyzed the consequences of chitin absence in the embryo of Drosophila melanogaster caused by mutations in the Chitin Synthase-1 (CS-1) gene, called krotzkopf verkehrt (kkv). Our histological data confirm that chitin is essential for procuticle integrity and further demonstrate that an intact procuticle is important to assemble and to stabilize the chitin-less epicuticle. Moreover, the phenotype of CS-1/kkv mutant embryos indicates that chitin is required to attach the cuticle to the epidermal cells, thereby maintaining epidermal morphology. Finally, sclerotization and pigmentation, which are the last steps in cuticle differentiation, are impaired in tissues lacking CS-1/kkv function, suggesting that proper cuticle structure is crucial for the activity of the underlying enzymes. Copyright 2005 Wiley-Liss, Inc.

                Author and article information

                Contributors
                Role: Academic Editor
                Journal
                Toxins (Basel)
                Toxins (Basel)
                toxins
                Toxins
                MDPI
                2072-6651
                24 September 2015
                October 2015
                : 7
                : 10
                : 3876-3886
                Affiliations
                Institute of Oceanology, Chinese Academy of Sciences, 7 Nanhai Road, Qingdao 266071, China; E-Mails: yuhuahua@ 123456qdio.ac.cn (H.Y.); rongfengli@ 123456qdio.ac.cn (R.L.); chenxl@ 123456qdio.ac.cn (X.C.); buqun08@ 123456163.com (Y.Y.); xingronge@ 123456qdio.ac.cn (R.X.); sliu@ 123456qdio.ac.cn (S.L.)
                Author notes
                [* ]Author to whom correspondence should be addressed; E-Mail: pcli@ 123456qdio.ac.cn ; Tel./Fax: +86-532-8289-8707.
                Article
                toxins-07-03876
                10.3390/toxins7103876
                4626708
                26404374
                0629366e-06cd-4d15-86c9-74a193704bd6
                © 2015 by the authors; licensee MDPI, Basel, Switzerland.

                This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license ( http://creativecommons.org/licenses/by/4.0/).

                History
                : 10 July 2015
                : 17 September 2015
                Categories
                Article

                Molecular medicine
                venom,jellyfish,nemopilema nomurai,toxicity,bombyx mori l.
                Molecular medicine
                venom, jellyfish, nemopilema nomurai, toxicity, bombyx mori l.

                Comments

                Comment on this article

                Related Documents Log