Differential protease activity augments polyphagy in Helicoverpa armigera

被引:47
作者
Chikate, Y. R. [1 ]
Tamhane, V. A. [1 ]
Joshi, R. S. [1 ]
Gupta, V. S. [1 ]
Giri, A. P. [1 ]
机构
[1] CSIR Natl Chem Lab, Plant Mol Biol Unit, Div Biochem Sci, Pune 411008, Maharashtra, India
关键词
Helicoverpa armigera; trypsin; chymotrypsin; polyphagy; adaptation; PLANT PROTEINASE-INHIBITORS; GENE-EXPRESSION PATTERNS; GUT PROTEINASES; IN-VITRO; DIGESTIVE ENZYMES; AGROTIS-IPSILON; TRYPSIN; MIDGUT; CHYMOTRYPSIN; LARVAE;
D O I
10.1111/imb.12018
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Helicoverpa armigera (Lepidoptera: Noctuidae) and other polyphagous agricultural pests are extending their plant host range and emerging as serious agents in restraining crop productivity. Dynamic regulation, coupled with a diversity of digestive and detoxifying enzymes, play a crucial role in the adaptation of polyphagous insects. To investigate the functional intricacy of serine proteases in the development and polyphagy of H.armigera, we profiled the expression of eight trypsin-like and four chymotrypsin-like phylogenetically diverse mRNAs from different life stages of H.armigera reared on nutritionally distinct host plants. These analyses revealed diet- and stage-specific protease expression patterns. The trypsins expressed showed structural variations, which might result in differential substrate specificity and interaction with inhibitors. Protease profiles in the presence of inhibitors and their mass spectrometric analyses revealed insight into their differential activity. These findings emphasize the differential expression of serine proteases and their consequences for digestive physiology in promoting polyphagy in H.armigera.
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页码:258 / 272
页数:15
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