Cloning and characterization of chymotrypsin- and trypsin-like cDNAs from the gut of the Hessian fly [ (say)]

Zhu, Yu Cheng; Xiang, Liu; Maddur, Ashoka A.; Oppert, Brenda; Chen, Ming‐Shun

doi:10.1016/j.ibmb.2004.09.006

Cited by 58 publications

(53 citation statements)

References 45 publications

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“…Furthermore, the transcripts of Hi-SP1 were not detected in adult tissues. Thus, it is possible that Hi-SP1 may be a larval specific gene, similar to chymotrypsins reported from the cotton bollworm (14) and the Hessian fly (15).…”

Section: Discussionmentioning

confidence: 59%

Characterization of the molecular features and expression patterns of two serine proteases in Hermetia illucens (Diptera: Stratiomyidae) larvae

Kim¹,

Bae²,

Kim³

et al. 2011

BMB Reports

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To investigate the molecular scavenging capabilities of the larvae of Hermetia illucens, two serine proteases (SPs) were cloned and characterized. Multiple sequence alignments and phylogenetic tree analysis of the deduced amino acid sequences of Hi-SP1 and Hi-SP2 were suggested that Hi-SP1 may be a chymotrypsin-and Hi-SP2 may be a trypsin-like protease. Hi-SP1 and Hi-SP2 3-D homology models revealed that a catalytic triad, three disulfide bonds, and a substrate-binding pocket were highly conserved, as would be expected of a SP. E. coli expressed Hi-SP1 and Hi-SP2 showed chymotrypsin or trypsin activities, respectively. Hi-SP2 mRNAs were consistently expressed during larval development. In contrast, the expression of Hi-SP1 mRNA fluctuated between feeding and molting stages and disappeared at the pupal stages. These expression pattern differences suggest that Hi-SP1 may be a larval specific chymotrypsin-like protease involved with food digestion, while Hi-SP2 may be a trypsin-like protease with diverse functions at different stages. [BMB reports 2011; 44(6): 387-392]

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Section: Discussionmentioning

confidence: 59%

Characterization of the molecular features and expression patterns of two serine proteases in Hermetia illucens (Diptera: Stratiomyidae) larvae

Kim¹,

Bae²,

Kim³

et al. 2011

BMB Reports

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“…Levels of the digestive enzymes trypsin-and chymotrypsin-like Ser proteases are low in neonate Hessian fly larvae that have not fed on plants. But in the Avirulent biotype L larvae on resistant H9-Iris seedlings 6 16 13.1 6 1.0 (16) gut of virulent larvae, the levels of these digestive enzymes increase over time (Shukle et al, 1985;Zhu et al, 2005), just as in the gut of another dipteran, the tsetse fly (Glossina morsitans), in which Ser proteases are induced by feeding (Yan et al, 2001). An induction of digestive enzymes may be responsible for the differing banding patterns of HFR1 proteolytic products observed in immunodetection experiments with virulent and avirulent larvae.…”

Section: Discussionmentioning

confidence: 99%

Functional Characterization of HFR1, a High-MannoseN-Glycan-Specific Wheat Lectin Induced by Hessian Fly Larvae

et al. 2008

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We previously cloned and characterized a novel jacalin-like lectin gene from wheat (Triticum aestivum) plants that responds to infestation by Hessian fly (Mayetiola destructor) larvae, a major dipteran pest of this crop. The infested resistant plants accumulated higher levels of Hfr-1 (for Hessian fly-responsive gene 1) transcripts compared with uninfested or susceptible plants. Here, we characterize the soluble and active recombinant His 6 -HFR1 protein isolated from Escherichia coli. Functional characterization of the protein using hemagglutination assays revealed lectin activity. Glycan microarray-binding assays indicated strong affinity of His 6 -HFR1 to Mana1-6(Mana1-3)Man trisaccharide structures. Resistant wheat plants accumulated high levels of HFR1 at the larval feeding sites, as revealed by immunodetection, but the avirulent larvae were deterred from feeding and consumed only small amounts of the lectin. Behavioral studies revealed that avirulent Hessian fly larvae on resistant plants exhibited prolonged searching and writhing behaviors as they unsuccessfully attempted to establish feeding sites. During His 6 -HFR1 feeding bioassays, Drosophila melanogaster larvae experienced significant delays in growth and pupation, while percentage mortality increased with progressively higher concentrations of His 6 -HFR1 in the diet. Thus, HFR1 is an antinutrient to dipteran larvae and may play a significant role in deterring Hessian fly larvae from feeding on resistant wheat plants.

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“…Interestingly, two additional disulphide bridges at Cys 22 -Cys 157 and Cys 127 -Cys 232 were reported in vertebrates (Rawlings & Barrett 1994) to anchor the pro-peptide to the protein core (Botos et al 2000). These variations indicate the evolutionary importance of SPs, but the exact role and pairing mechanism of these cysteine residues are still unclear (Zhu et al 2005).…”

Section: Discussionmentioning

confidence: 99%

Striped murrel S1 family serine protease: immune characterization, antibacterial property and enzyme activities

et al. 2014

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Abstract:We report a molecular characterization of S1 family serine protease (SP-1) from snakehead murrel (or called striped murrel) Channa striatus (Cs). CsSP-1 polypeptide contained a catalytic core domain (otherwise known as serine protease trypsin domain) between H 20 and I 237 along with a catalytic triad at H 61 , D 104 and S 197 . Phylogenetic analysis confirmed that CsSP-1 belongs to serine protease S1 family. The tertiary structure showed that CsSP-1 contains 14 β-sheets as 2 separate β-barrels (the first β-barrel consists of 8 β-sheets in the N-terminal region and the second β-barrel consists of 6 β-sheets in the C-terminal region) and 3 α-helical regions. Significantly (P < 0.05) the highest CsSP-1 mRNA expression was observed in intestine, liver and kidney, moderate expression was seen in spleen, head kidney, skin and blood, and the lowest one in brain, gill, muscle and heart. Further, the expression was induced in intestine with fungus Aphanomyces invadans and bacteria Aeromonas hydrophila. The recombinant CsSP-1 protein showed antibacterial activity against both gram-negative and gram-positive bacteria. The optimum CsSP-1 enzyme activity against the substrate casein was determined at 8 mM casein concentration. Moreover, the activity was highly influenced by 5 mM phenyl-methylsulfonyl fluoride followed by ethylenediaminetetraacetic acid, 4-(2-aminoethyl)benzenesulfonylfluoride hydrochloride and calpain inhibitor I. The CsSP-1 enzyme exhibited the highest activity at pH 7.5 and temperature 35• C. The overall results showed the potential involvement of CsSP-1 in the immune system of murrels. However, further research is necessary to study the mechanism of implicit trypsin association in the defence process.

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Cloning and characterization of chymotrypsin- and trypsin-like cDNAs from the gut of the Hessian fly [ (say)]

Cited by 58 publications

References 45 publications

Characterization of the molecular features and expression patterns of two serine proteases in Hermetia illucens (Diptera: Stratiomyidae) larvae

Characterization of the molecular features and expression patterns of two serine proteases in Hermetia illucens (Diptera: Stratiomyidae) larvae

Functional Characterization of HFR1, a High-MannoseN-Glycan-Specific Wheat Lectin Induced by Hessian Fly Larvae

Striped murrel S1 family serine protease: immune characterization, antibacterial property and enzyme activities

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