49
views
0
recommends
+1 Recommend
1 collections
    0
    shares
      • Record: found
      • Abstract: not found
      • Article: not found

      Mode of action of Bacillus thuringiensis Cry and Cyt toxins and their potential for insect control

      , ,
      Toxicon
      Elsevier BV

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          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

          Bacillus thuringiensis Crystal (Cry) and Cytolitic (Cyt) protein families are a diverse group of proteins with activity against insects of different orders--Lepidoptera, Coleoptera, Diptera and also against other invertebrates such as nematodes. Their primary action is to lyse midgut epithelial cells by inserting into the target membrane and forming pores. Among this group of proteins, members of the 3-Domain Cry family are used worldwide for insect control, and their mode of action has been characterized in some detail. Phylogenetic analyses established that the diversity of the 3-Domain Cry family evolved by the independent evolution of the three domains and by swapping of domain III among toxins. Like other pore-forming toxins (PFT) that affect mammals, Cry toxins interact with specific receptors located on the host cell surface and are activated by host proteases following receptor binding resulting in the formation of a pre-pore oligomeric structure that is insertion competent. In contrast, Cyt toxins directly interact with membrane lipids and insert into the membrane. Recent evidence suggests that Cyt synergize or overcome resistance to mosquitocidal-Cry proteins by functioning as a Cry-membrane bound receptor. In this review we summarize recent findings on the mode of action of Cry and Cyt toxins, and compare them to the mode of action of other bacterial PFT. Also, we discuss their use in the control of agricultural insect pests and insect vectors of human diseases.

          Related collections

          Author and article information

          Journal
          Toxicon
          Toxicon
          Elsevier BV
          00410101
          March 2007
          March 2007
          : 49
          : 4
          : 423-435
          Article
          10.1016/j.toxicon.2006.11.022
          1857359
          17198720
          756e16a3-f61c-44ef-9ebf-2af190794dcc
          © 2007

          https://www.elsevier.com/tdm/userlicense/1.0/

          History

          Comments

          Comment on this article