Heterodera glycines cysts contain an extensive array of endoproteases as well as inhibitors of proteases in H. glycines and Meloidogyne incognita infective juvenile stages
| Autor: | David J. Chitwood, Edward P. Masler |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
chemistry.chemical_classification Proteases Protease biology Heterodera medicine.medical_treatment biology.organism_classification Trypsin Serine 03 medical and health sciences 030104 developmental biology Enzyme chemistry Biochemistry Meloidogyne incognita medicine Agronomy and Crop Science Ecology Evolution Behavior and Systematics Terra incognita medicine.drug |
| Zdroj: | Nematology. 18:489-499 |
| ISSN: | 1568-5411 |
| DOI: | 10.1163/15685411-00002972 |
| Popis: | Heterodera glycinescysts contain proteases, and inhibitors of protease activities in various nematode species. In this investigation, proteases inH. glycinescysts were identified using a commercially available FRET-peptide library comprising 512 peptide pools qualified to detect up to four endoprotease types (aspartic, cysteine, metallo- and serine). Native cyst content (nHglCE) digested peptides in over 96% of the pools with all four protease types identified. Serine and metalloproteases represented nearly 70% of all proteases detected and were examined further. Trypsin (serine) and matrix metalloprotease (MMP) activities were compared among nHglCE, andH. glycinessecond-stage juvenile (J2) andMeloidogyne incognitaJ2 extracts. The relative levels of activity were different for all three enzyme sources. Trypsin activity was up to 60-fold greater inM. incognitathan in eitherH. glycinessource, while MMP activity was highest in nHglCE and lowest inM. incognitaJ2. Heat-denatured cyst content (hHglCE) inhibited proteases in all three nematode preparations and was generally greater inM. incognitathan inH. glycines. Largest differences (5.2- to 6.4-fold) were observed betweenM. incognitaand nHglCE trypsin and MMP inhibition. In infective juveniles, hHglCE inhibitedM. incognitaJ2 trypsin (IC50 = 0.64 hHglCEeq reaction−1) and MMP (IC50 = 0.54) more potently than eitherH. glycinestrypsin (IC50 = 1.34) or MMP (IC50 = 1.84). Use of three MMP substrates (73, 74 and 80) revealed clear species differences as well as complex associations between activity and inhibition. MMP73 digestion rates were the same inH. glycinesandM. incognitabut responses to hHglCE inhibition were different. MMP80 digestion rates were different but inhibition was the same. MMP74 digestion rates and inhibition levels were each different between species. These experiments provide further evidence that theH. glycinescyst should be examined as a source of compounds useful for developing nematode control methods. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|