期刊
INSECT SCIENCE
卷 28, 期 3, 页码 692-704出版社
WILEY
DOI: 10.1111/1744-7917.12791
关键词
chitin; chitinase; chitin binding; degradation; multiple module; synergy
类别
资金
- National Key R&D Program of China [2017YFD0201207]
- Natural Science Foundation of China [31402015, 31830076]
- State Key Laboratory for Biology of Plant Diseases and Insect Pests [SKLOF201801]
- Shenzhen Science and Technology Program [KQTD20180411143628272]
The insect group II chitinase plays an important role in insect molting and acts synergistically with other chitinases to degrade cuticular chitin efficiently.
The insect group II chitinase (ChtII, also known as Cht10) is a unique chitinase with multiple catalytic and chitin-binding domains. It has been proven genetically to be an essential chitinase for molting. However, ChtII's role in chitin degradation during insect development remains poorly understood. Obtaining this knowledge is the key to fully understanding the chitin degradation system in insects. Here, we investigated the role of OfChtII during the molting ofOstrinia furnacalis, a model lepidopteran pest insect. OfChtII was expressed earlier than OfChtI (OfCht5) and OfChi-h, at both the gene and protein levels during larva-pupa molting as evidenced by quantitative polymerase chain reaction and western blot analyses. A truncated OfChtII, OfChtII-B4C1, was recombinantly expressed inPichia pastoriscells and purified to homogeneity. The recombinant OfChtII-B4C1 loosened compacted chitin particles and produced holes in the cuticle surface as evidenced by scanning electron microscopy. It synergized with OfChtI and OfChi-h when hydrolyzing insoluble alpha-chitin. These findings suggested an important role for ChtII during insect molting and also provided a strategy for the coordinated degradation of cuticular chitin during insect molting by ChtII, ChtI and Chi-h.
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