Proteomic analysis of the peritrophic matrix from the gut of the caterpillar, Helicoverpa armigera
| Autor: | Anh T. Cao, Karl H.J. Gordon, Peter D. East, Eric R. Hines, Peter M. Campbell |
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| Rok vydání: | 2008 |
| Předmět: |
Proteome
Gene Expression Chitin macromolecular substances Moths Helicoverpa armigera Biochemistry Aminopeptidase chemistry.chemical_compound Bacillus thuringiensis Animals Peritrophic matrix Molecular Biology Gel electrophoresis biology fungi biology.organism_classification Chitin deacetylase Gastrointestinal Tract chemistry Larva Insect Science Insect Proteins |
| Zdroj: | Insect Biochemistry and Molecular Biology. 38:950-958 |
| ISSN: | 0965-1748 |
| DOI: | 10.1016/j.ibmb.2008.07.009 |
| Popis: | The peritrophic matrix from the midgut of the caterpillar, Helicovera armigera, was solubilized by treatment with anhydrous trifluoromethanesulfonic acid, apparently by depolymerisation of its chitin component. This allowed the efficient extraction of proteins in a technique that may be broadly applicable to the analysis of other structures containing chitin. Gel electrophoresis and mass spectrometry of tryptic peptides were used to identify the extracted proteins with gut-expressed cDNA sequences. The major proteins of this cohesive, digestion-resistant structure are chitin deacetylase-like and mucin-like proteins, the latter with multiple chitin-binding domains that may cross-link chitin fibrils to provide a barrier against abrasive food particles and parasites, one of the major functions of the matrix. Other proteins found in the H. armigera gut peritrophic matrix suggest that the matrix is a dynamic, complex structure that may participate in the immobilization of digestive enzymes, actively protect the gut from parasite invasion and intercept toxins such as lectins and Bacillus thuringiensis crystal proteins. |
| Databáze: | OpenAIRE |
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