redivivus and Caenorhabditis elegans ( Yang et al., 2007c). redivivus and immobilize the free-living nematodes P. varietas could degrade casein, gelatin, BSA (bovine serum albumin), hydrolyze the purified cuticle of P. The protein can degrade not only casein, gelatin, bovine serum albumin, collagen and nematode cuticles, but also immobilize the free living nematode Panagrellus redivivus and the pine wood nematode Bursaphelenchus xylophilus ( Yang et al., 2007b). Ac1 has a molecular mass of 35 kDa, optimum activity at pH 7.0 and 53.2☌. The nematotoxic activity of Lmz1 involving in fungal infection was confirmed by nematode-immobilisation, cuticle degradation and immunodepletion ( Zhao et al., 2005). Lmz1 showed a molecular mass of approximately 33 kDa, pI 10.5, optimal activity of Lmz1 at 60☌ and pH 11-12. Hasp and Hnsp, with molecular weights of 33 and 32 kDa, optimal temperatures of 75 and 40☌ and optimal pH of 9 and 7, respectively, digested cuticle proteins in vitro ( Wang et al., 2007, 2009). conoides have been analyzed ( Wang et al., 2007, 2009 Zhao et al., 2005 Yang et al., 2007b, c). Recently, an alkaline serine proteinase Hasp and a neutral serine proteinase Hnsp from the endoparasite Hirsutella rhossiliensis, Dv1 from the nematode-trapping fungus Dactylellina varietas, Lmz1 from the toxic fungus Clonostachys rosea and an extracellular serine protease Ac1 from the nematode trapping fungus A. At least 16 proteinases of nematophagous fungi, all of which were serine proteinases, homologous to each other and belong to proteinase K family (Peptidase_S8, Subtilase) ( Tunlid et al., 1994 Segers et al., 1995 Bonants et al., 1995), were purified and characterized ( Huang et al., 2004 Yang et al., 2007a). The cuticle and egg shell of nematodes activates the expression of the enzymes ( Tunlid et al., 1994 Ahman et al., 1996). The proteinases of nematophagous fungi which digest the cuticle or egg shell, are the characteristics of virulence. During the process of penetration by nematophagous fungi, the roles of secreted hydrolytic enzymes are very important. The mechanisms by which nematophagous fungi infect nematodes have been the basis for development of genetically engineered strains which are able to control parasitic nematodes more effectively than wild types. However, these bio-pesticides cannot control nematodes quickly now. robusta ( Cayrol et al., 1978) and Paecilomyces lilacinus ( Davide and Zorilla, 1983) have been developed as commercial products. Nematophagous fungi, for example, Arthrobotrys irregularis ( Cayrol, 1983), A. Asian Journal of Biological Sciences, 7: 76-110.īiocontrol agents provide an environmentally friendly and effective management of plant parasitic nematodes. Cloning, Homology Modeling and Active Site Prediction of Secreted Serine Proteinase (PrDI) and Carboxylesterase (CaDI) Gene from Nematophagous Fungi DactylellinaĬionopaga. Was identified by docking of the heptapeptide inhibitor Pro-Ala-Pro-Phe-Ala-Ser-Ala.Ĭomparison of the substrate-binding sites of PrDI with those of PR1, Ver112Īnd VCP1, the serine proteinases from nematophagous fungi and entomopathogenicįungus, showed that the catalytic regions among these serine proteinases were Probably catalyzed the long-chain carboxylester. Pathogen of pests, might be butyrylcholinesterase and acetylcholinesterase and That the protein was more similar to the carboxylesterase and lipases of fungal Its active sites of CaDI with other lipases and carboxylesterases indicated Ser225, Glu358 and His470 consisted of the active ![]() The genes presented the enhanced expression when Dactylellina cionpaga wasĬultured on water agar containing Caenorhabditis elegans in contrast ![]() Respectively, were cloned and characterized by phylogeny and structural comparison. Genes encoding a secreted serine proteinase (PrDI) and a carboxylesterase (CaDI), Nematophagous fungi are important biocontrol agents of nematode pests.
0 Comments
Leave a Reply. |
AuthorWrite something about yourself. No need to be fancy, just an overview. ArchivesCategories |