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Identification of the Mamestra configurata (Lepidoptera Noctuidae) peritrophic matrix proteins and enzymes involved in peritrophic matrix chitin metabolism - Identification of the Mamestra configurata (Lepidoptera Noctuidae) peritrophic matrix proteins and enzymes involved in peritrophic matrix chitin metabolism

Umut ; Toprak ; Martin ; Erlandson ; Doug ; Baldwin ; Steve ; Karcz ; Lianglu ; Wan ; Cathy ; Coutu ; Cedric ; Gillott ; Dwayne ; D. ; Hegedus

中国昆虫科学:英文版 - Insect Science, 2016, Issue 05, pp.656-674 [Rivista Peer Reviewed]

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  • Titolo:
    Identification of the Mamestra configurata (Lepidoptera Noctuidae) peritrophic matrix proteins and enzymes involved in peritrophic matrix chitin metabolism - Identification of the Mamestra configurata (Lepidoptera Noctuidae) peritrophic matrix proteins and enzymes involved in peritrophic matrix chitin metabolism
  • Autore: Umut ; Toprak ; Martin ; Erlandson ; Doug ; Baldwin ; Steve ; Karcz ; Lianglu ; Wan ; Cathy ; Coutu ; Cedric ; Gillott ; Dwayne ; D. ; Hegedus
  • Descrizione: The peritrophic matrix (PM) is essential for insect digestive system physiol- ogy as it protects the midgut epithelium from damage by food particles, pathogens, and toxins. The PM is also an attractive target for development of new pest control strategies due to its per os accessibility. To understand how the PM performs these functions, the molecular architecture of the PM was examined using genomic and proteomic approaches in Mamestra configurata (Lepidoptera: Noctuidae), a major pest of cruciferous oilseed crops in North America. Liquid chromatography-tandem mass spectrometry analyses of the PM identified 82 proteins classified as: (i) peritrophins, including a new class with a CBDIII domain; (ii) enzymes involved in chitin modification (chitin deacetylases), di- gestion (serine proteases, aminopeptidases, carboxypeptidases, lipases and ~-amylase) or other reactions (/~-l,3-glucanase, alkaline phosphatase, dsRNase, astacin, pantetheinase); (iii) a heterogenous group consisting of polycalin, REPATs, serpin, C-Type lectin and Lsti99/Lsti201 and 3 novel proteins without known orthologs. The genes encoding PM proteins were expressed predominantly in the midgut, cDNAs encoding chitin synthase-2 (McCHS-2), chitinase (McCHI), and fl-N-acetylglucosaminidase (McNAG) enzymes, in- volved in PM chitin metabolism, were also identified. McCHS-2 expression was specific to the midgut indicating that it is responsible for chitin synthesis in the PM, the only chitinous material in the midgut. In contrast, the genes encoding the chitinolytic enzymes were expressed in multiple tissues. McCHS-2, McCHI, and McNAG were expressed in the midgut of feeding larvae, and NAG activity was present in the PM. This information was used to generate an updated model of the lepidopteran PM architecture.
  • Fa parte di: 中国昆虫科学:英文版 - Insect Science, 2016, Issue 05, pp.656-674
  • Soggetti: Chitin; Mamestra Configurata; Peritrophic Matrix; Protein
  • Titoli correlati: 作者单位: Agriculture and Agri-Food Canada, Saskatoon, SK, Canada Department of Biology, University of Saskatchewan, Saskatoon, SK, Canada Department of Plant Protection, Faculty of Agriculture, University of Ankara, Ankara, Turkey Department of Food and Bioproduct Sciences, University of Saskatchewan, Saskatoon, SK, Canada plant Biotechnology Institute, National Research Council of Canada, Saskatoon, SK, Canada
  • Identificativo: ISSN: 1672-9609
  • Fonte: 维普数据 (Chongqing VIP Information Co.)

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