Cloning and characterization of cDNAS encoding carboxypeptidase-like proteins from the gut of Hessian fly larvae [Mayetiola destructor (Say)]☆

Xiang, Liu; Fellers, John P.; Zhu, Yu Cheng; Mutti, Navdeep S.; El‐Bouhssini, M.; Chen, Ming‐Shun

doi:10.1016/j.ibmb.2006.05.008

Cited by 10 publications

(12 citation statements)

References 46 publications

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“…Following this approach, we sequenced 1015 cDNA clones from a gut cDNA library derived from 1st instar Hessian fly larvae. Since the insect gut is the major digestive, and one of the major detoxification sites, we identified a high percentage of cDNA clones that corresponded to genes encoding digestive and detoxification enzymes, as expected (Zhu et al, 2005;Liu et al, 2006). However, to our surprise, there was a group of cDNAs (characterized in this paper) that was even more abundant than the cDNAs representing genes of digestive enzymes.…”

Section: Discussionsupporting

confidence: 54%

“…These two related groups of cDNAs were selected for further analysis because they were the most abundant in terms of transcripts, representing 7.2% of the total sequenced cDNA clones. For comparison, the next most abundant group, the cDNAs encoding digestive proteases including trypsins, chymotrypsins, and carboxypeptidases, only represented 5.1% of total sequenced cDNA clones (Zhu et al, 2005;Liu et al, 2006).…”

Section: Resultsmentioning

confidence: 99%

“…Full length sequences of 1015 random cDNA clones were obtained from this library. Many of them encode digestive proteases including trypsins, chymotrypsins, and carboxypeptiases (Zhu et al, 2005;Liu et al, 2006). In this paper, we report the isolation and characterization of a group of genes that encode small secreted proteins of unknown function from the gut of Hessian fly larvae.…”

Section: Introductionmentioning

confidence: 99%

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Genes encoding a group of related small secreted proteins from the gut of Hessian fly larvae [Mayetiola destructor (Say)]

et al. 2006

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A group of related genes has been isolated and characterized from the gut of Hessian fly larvae [Mayetiola destructor (Say)]. Members in this group appear to encode proteins with secretary signal pep tides at the N‐terminals. The mature putative proteins are small, acidic proteins with calculated molecular masses of 14.5 to 15.3 kDa, and isoelectric points from 4.56 to 4.88. Northern blot analysis revealed that these genes are expressed predominantly in the gut of Hessian fly larvae and pupae. Two related genes, G10K1 and G10K2, were isolated as tandem repeats. Both genes contain three exons and two introns. The intron/exon boundaries were conserved in terms of amino acid encoding, suggesting that they arose by gene duplication. The fact that the frequency of this group of clones in a gut cDNA library higher than that of total cDNA clones encoding digestive enzymes suggested that this group of proteins may perform an important function in the gut physiology of this insect. However, the exact functions of these proteins are as yet known since no sequence similarity could be identified between these proteins and any known sequences in public databases using standard methods.

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Section: Discussionsupporting

confidence: 54%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Genes encoding a group of related small secreted proteins from the gut of Hessian fly larvae [Mayetiola destructor (Say)]

et al. 2006

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“…Alignments were made with Te. molitor CPAs and CPA from A. aegypti (AaCPA, Edwards et al ., 1997), Culicoides sonorensis (CsCPA, Campbell et al ., 2000), D. melanogaster (DmCPA, Adams et al ., 2005), Helicoverpa armigera (HaCPA1 and 2, Bown & Gatehouse, 2004), Mayetiola destructor (MdCPA1‐5, Liu et al. , 2006), Sitodiplosis mosellana (SmCPA, Mittapalli et al ., 2006), Simulium vittatum (ScCPA, Ramos et al ., 1993), Trichoplusia ni (TnCPA1‐5, Wang et al.…”

Section: Resultsmentioning

confidence: 99%

Sequence analysis and molecular characterization of larval midgut cDNA transcripts encoding peptidases from the yellow mealworm, Tenebrio molitor L.

Prabhakar

Chen

Elpidina

et al. 2007

Insect Molecular Biology

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Peptidase sequences were analysed in randomly picked clones from cDNA libraries of the anterior or posterior midgut or whole larvae of the yellow mealworm, Tenebrio molitor Linnaeus. Of a total of 1528 sequences, 92 encoded potential peptidases, from which 50 full-length cDNA sequences were obtained, including serine and cysteine proteinases and metallopeptidases. Serine proteinase transcripts were predominant in the posterior midgut, whereas transcripts encoding cysteine and metallopeptidases were mainly found in the anterior midgut. Alignments with other proteinases indicated that 40% of the serine proteinase sequences were serine proteinase homologues, and the remaining ones were identified as either trypsin, chymotrypsin or other serine proteinases. Cysteine proteinase sequences included cathepsin B- and L-like proteinases, and metallopeptidase transcripts were similar to carboxypeptidase A. Northern blot analysis of representative sequences demonstrated the differential expression profile of selected transcripts across five developmental stages of Te. molitor. These sequences provide insights into peptidases in coleopteran insects as a basis to study the response of coleopteran larvae to external stimuli and to evaluate regulatory features of the response.

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“…In Hessian flies ( Mayetiola destructor [Say]), one of the most destructive pests of wheat, nine cDNAs of carboxypeptidases were characterized. Of the nine carboxypeptidases, A1 and B functioned as major digestive enzymes in the gut; however, the other carboxypeptidases probably served as regulators of insect development in addition to being potential digestive proteases (Liu et al. , 2006b).…”

Section: Introductionmentioning

confidence: 99%

Characterization and influences of classical insect hormones on the expression profiles of a molting carboxypeptidase A from the cotton bollworm (Helicoverpa armigera)

Sui

Liu

Chai

et al. 2009

Insect Molecular Biology

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Molting is a very important physiological behavior to arthropods. During molting, integument apolysis occurs, which is the digestion and absorption of the old endocuticle for new cuticle formation. Proteases play critical roles in this process. Molting carboxypeptidase A ( Ha-CPA ) is characterized from Helicoverpa armigera . The Ha-CPA transcript was mainly present in the integument from the 5th instar larvae. In the integument, the transcription level of the gene reached its peak at the 5th instar molting stage and the 6th instar prepupal stage, respectively. The examination of immunohistochemistry revealed that Ha-CPA could distribute into the molting fluid in the molting-and prepupal-stage larvae. The expression of Ha-CPA could be up-regulated by 20-hydroxyecdysone (20E). These facts indicate that Ha-CPA participates in the apolysis of the integument during larval molting and metamorphosis.

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Cloning and characterization of cDNAS encoding carboxypeptidase-like proteins from the gut of Hessian fly larvae [Mayetiola destructor (Say)]☆

Cited by 10 publications

References 46 publications

Genes encoding a group of related small secreted proteins from the gut of Hessian fly larvae [Mayetiola destructor (Say)]

Genes encoding a group of related small secreted proteins from the gut of Hessian fly larvae [Mayetiola destructor (Say)]

Sequence analysis and molecular characterization of larval midgut cDNA transcripts encoding peptidases from the yellow mealworm, Tenebrio molitor L.

Characterization and influences of classical insect hormones on the expression profiles of a molting carboxypeptidase A from the cotton bollworm (Helicoverpa armigera)

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