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.
Highlights
Serine proteases, ubiquitous enzymes found in eukaryotes, bacteria, and viruses, constitute almost one‐third of all proteases and play a pivotal role in the catalysis of intracellular and extracellular hydrolytic reactions (Yang et al, 2017)
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
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
Summary
Ubiquitous enzymes found in eukaryotes, bacteria, and viruses, constitute almost one‐third of all proteases and play a pivotal role in the catalysis of intracellular and extracellular hydrolytic reactions (Yang et al, 2017). Serine proteases are known to be involved in a wide range of essential biological processes (Ross et al, 2003; Zou et al, 2006; Zhao et al, 2010) In addition to their vital role in physiological processes, the activity of these proteases, if not controlled properly, might be hazardous to living organisms (Neurath, 1989). Injury due to excessive protease activity includes tissue damage, melanization, and inappropriate coagulation, among others (Gubb et al, 2010; Eleftherianos and Revenis, 2011) Their activity must be properly and strictly controlled by inhibitors (Krowarsch et al, 2003; Rawlings et al, 2004). After successful cleavage of the scissile bonds, serpin dramatically undergoes a conformational change that covalently traps the target proteinase (Dissanayake et al, 2006; Ulvila et al, 2011; Yang et al, 2017)
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