Premium
Differential protease activity augments polyphagy in H elicoverpa armigera
Author(s) -
Chikate Y. R.,
Tamhane V. A.,
Joshi R. S.,
Gupta V. S.,
Giri A. P.
Publication year - 2013
Publication title -
insect molecular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.955
H-Index - 93
eISSN - 1365-2583
pISSN - 0962-1075
DOI - 10.1111/imb.12018
Subject(s) - biology , protease , proteases , trypsin , serine protease , chymotrypsin , enzyme , biochemistry
H elicoverpa armigera ( L epidoptera: N octuidae) 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 .