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

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 bollw...

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Main Author: Muhammad Shakeel
Format: Article
Language:English
Published: Instituto Internacional de Ecologia 2020-08-01
Series:Brazilian Journal of Biology
Subjects:
Online Access:http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1519-69842021000300516&tlng=en
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author Muhammad Shakeel
author_facet Muhammad Shakeel
author_sort Muhammad Shakeel
collection DOAJ
description 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.
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spelling doaj.art-ded649ad13de41f8885e9af67bdf84712022-12-21T19:29:10ZengInstituto Internacional de EcologiaBrazilian Journal of Biology1678-43752020-08-0181351652510.1590/1519-6984.223579Molecular identification, characterization, and expression analysis of a serine protease inhibitor gene from cotton bollworm, Helicoverpa armigera (Lepidoptera: Noctuidae)Muhammad Shakeelhttps://orcid.org/0000-0002-8515-0053Abstract 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.http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1519-69842021000300516&tlng=encloningmRNA expressionreactive center loopserpinfat body
spellingShingle Muhammad Shakeel
Molecular identification, characterization, and expression analysis of a serine protease inhibitor gene from cotton bollworm, Helicoverpa armigera (Lepidoptera: Noctuidae)
Brazilian Journal of Biology
cloning
mRNA expression
reactive center loop
serpin
fat body
title Molecular identification, characterization, and expression analysis of a serine protease inhibitor gene from cotton bollworm, Helicoverpa armigera (Lepidoptera: Noctuidae)
title_full Molecular identification, characterization, and expression analysis of a serine protease inhibitor gene from cotton bollworm, Helicoverpa armigera (Lepidoptera: Noctuidae)
title_fullStr Molecular identification, characterization, and expression analysis of a serine protease inhibitor gene from cotton bollworm, Helicoverpa armigera (Lepidoptera: Noctuidae)
title_full_unstemmed Molecular identification, characterization, and expression analysis of a serine protease inhibitor gene from cotton bollworm, Helicoverpa armigera (Lepidoptera: Noctuidae)
title_short Molecular identification, characterization, and expression analysis of a serine protease inhibitor gene from cotton bollworm, Helicoverpa armigera (Lepidoptera: Noctuidae)
title_sort molecular identification characterization and expression analysis of a serine protease inhibitor gene from cotton bollworm helicoverpa armigera lepidoptera noctuidae
topic cloning
mRNA expression
reactive center loop
serpin
fat body
url http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1519-69842021000300516&tlng=en
work_keys_str_mv AT muhammadshakeel molecularidentificationcharacterizationandexpressionanalysisofaserineproteaseinhibitorgenefromcottonbollwormhelicoverpaarmigeralepidopteranoctuidae