Tripeptides derived from reactive centre loop of potato type II protease inhibitors preferentially inhibit midgut proteases of Helicoverpa armigera

2018 ◽  
Vol 95 ◽  
pp. 17-25 ◽  
Author(s):  
Nidhi S. Saikhedkar ◽  
Rakesh S. Joshi ◽  
Ashiwini S. Bhoite ◽  
Radhika Mohandasan ◽  
Amit Kumar Yadav ◽  
...  
Keyword(s):  
Protease Inhibitors ◽  
Helicoverpa Armigera ◽  
Type Ii ◽  
Reactive Centre Loop ◽  
Helicoverpa Armígera

The impact of ingested potato type II inhibitors on the production of the major serine proteases in the gut of Helicoverpa armigera

2013 ◽  
Vol 43 (2) ◽  
pp. 197-208 ◽  
Author(s):  
J.A. Stevens ◽  
K.M. Dunse ◽  
R.F. Guarino ◽  
B.L. Barbeta ◽  
S.C. Evans ◽  
...  
Keyword(s):  
Helicoverpa Armigera ◽  
Serine Proteases ◽  
Type Ii ◽  
Helicoverpa Armígera ◽  
The Impact

scholarly journals A strong inhibitor of chymotrypsin/elastase is highly antimetabolic to Helicoverpa armigera larvae

2002 ◽  
Vol 55 ◽  
pp. 421-428 ◽  
Author(s):  
L.N. Gatehouse ◽  
J.T. Christeller ◽  
H.S. Gatehouse ◽  
X.Y. Zou
Keyword(s):  
Protease Inhibitors ◽  
Helicoverpa Armigera ◽  
Active Site ◽  
Artificial Diet ◽  
Rna Expression ◽  
Strong Inhibitor ◽  
Experimental Animals ◽  
Gene Group ◽  
Polyamino Acid ◽  
Helicoverpa Armígera

Chymostatin is a small nonprotein polyamino acid that specifically inhibits chymotrypsinlike enzymes by covalently binding to their active site It is therefore a model for tightbinding proteinaceous protease inhibitors of chymotrypsin/elastase specificity The Lepidopteran Helicoverpa armigera was raised on an artificial diet containing 003 chymostatin After 14 days the experimental animals were approximately twentyfold smaller than the controls although there was no increase in mortality The RNA expression levels of the main trypsin gene group were found to decrease while that of the chymotrypsin/elastase gene group increased Changes in activity of the midgut protease enzymes did not correlate to these changes in RNA expression

scholarly journals Molecular identification, characterization, and expression analysis of a serine protease inhibitor gene from cotton bollworm, Helicoverpa armigera (Lepidoptera: Noctuidae)

2020 ◽  
Author(s):  
Muhammad Shakeel
Keyword(s):  
Protease Inhibitor ◽  
Serine Protease ◽  
Protease Inhibitors ◽  
Helicoverpa Armigera ◽  
Fat Body ◽  
Critical Role ◽  
Functional Characterization ◽  
Serine Protease Inhibitor ◽  
Cotton Bollworm ◽  
Helicoverpa Armígera

Abstract Serine protease inhibitors (serpins), a superfamily of protease inhibitors, are known to be involved in several physiological processes, such as development, metamorphosis, and innate immunity. In our study, a full-length serpin cDNA, designated Haserpin1, was isolated from the cotton bollworm Helicoverpa armigera. The cDNA sequence of Haserpin1 is 1176 nt long, with an open reading frame encoding 391 amino acids; there is one exon and no intron. The predicted molecular weight of Haserpin1 is 43.53 kDa, with an isoelectric point of 4.98. InterProScan was employed for Haserpin1 functional characterization, which revealed that Haserpin1 contains highly conserved signature motifs, including a reactive center loop (RCL) with a hinge region (E341–N350), the serpin signature, (F367–F375) and a predicted P1–P1′ cleavage site (L357–S358), which are useful for identifying serpins. Transcripts of Haserpin1 were constitutively expressed in the fat body, suggesting that it is the major site for serpin synthesis. During the developmental stages, a fluctuation in the expression level of Haserpin1 was observed, with low expression detected at the 5th-instar larval stage. In contrast, relatively high expression was detected at the prepupal stage, suggesting that Haserpin1 might play a critical role at the H. armigera wandering stage. Although the detailed function of this serpin (Haserpin1) needs to be elucidated, our study provides a perspective for the functional investigation of serine protease inhibitor genes.

Sign in / Sign up

Export Citation Format

Share Document