A molt-associated chitinase cDNA from the spruce budworm, Choristoneura fumiferana

Zheng, Y.-P.; Zheng, Sichun; Cheng, Xiao Wen; Ladd, Tim R.; Lingohr, Erika J.; Krell, Peter J.; Arif, Basil M.; Retnakaran, Arthur; Feng, Qili

doi:10.1016/s0965-1748(02)00166-2

Cited by 54 publications

(60 citation statements)

References 36 publications

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“…The catalytic domain of eukaryotic chitinases is known to be glycosylated with N-linkage. Although some reports have suggested one or two more putative N-glycosylation sites in the linker region (Ahmad et al, 2003;Kim et al, 1998;Zheng et al, 2002) and the substrate binding domain (Kramer et al, 1993), the sites did not appear to be common to all the confirmed lepidopteran chitinases. Only the two consensus sites in the catalytic domain (NFT, AA 87-89; NAT, AA 304-306) are confident (Fig.…”

Section: Resultsmentioning

confidence: 76%

“…6). The linker region not only connects the two domains, but also plays a role in the facilitation of enzyme secretion with a high amount of conjugated carbohydrate (Gopalakrishnan et al, 1995;Zheng et al, 2002). Although the linker region was the most divergent in amino acid sequence among the lepidopteran chitinases, 59.3% mean identity and 66.6% mean sum of identity and similarity (Table 1), the Oglycosylation-bearing serine and threonine residues were in consensus between the aligned sequences (Fig.…”

Section: Resultsmentioning

confidence: 98%

“…Sequence alignment, phylogenetic analysis, and hydropathy plotting All the analyses were performed using the tools contained in the MacVector 7.0 software suite (Oxford Molecular, USA) together with previously reported lepidopteran chitinases; the common cutworm (Spodoptera litura) from Shinoda et al (2001), the fall armyworm (Spodoptera frugiperda) from Bolognesi et al (2005), the cotton bollworm (Helicoverpa almigera) from Ahmad et al (2003), the tomato moth (Lacanobia oleracea) from Fitches et al (2004), the fall webworm (Hyphantria cunea) from Kim et al (1998), the tobacco hornworm (Manduca sexta) from Kramer et al (1993), the wild silkmoth (Bombyx mandarina) from Goo et al (1999), the silkworm (Bombyx mori) from Kim et al (1998), and the spruce budworm (Choristoneura fumiferana) from Zheng et al (2002).…”

Section: Real-time Quantitative Reverse Transcription Pcr (Rt-pcr) Anmentioning

confidence: 99%

“…Chitin degradation must be tightly regulated to maintain its role in insect development, and the transcription or enzyme activity of chitinase in integument is restricted to molting periods by hormonal regulation (Kramer et al, 1993;Zheng et al, 2002). Therefore, the chitin hydrolysis step has received significant attention as a potential target for pest management.…”

Section: Introductionmentioning

confidence: 99%

“…The lepidopteran chitinases have a common multi-domain structure with a catalytic region, a PEST-like region enriched in proline, glutamate, serine and threonine, and a cysteine-rich chitin-binding region (Ahmad et al, 2003;Bolognesi et al, 2005;Fitches et al, 2004;Goo et al, 1999;Kim et al, 1998;Shinoda et al, 2001;Zheng et al, 2002), but there are still some controversies on the border positions between domains.…”

Section: Introductionmentioning

confidence: 99%

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Molecular Cloning and Functional Expression of Chitinase-Encoding cDNA from the Cabbage Moth, Mamestra brassicae

Paek

Park

Jeong

2012

Molecules and Cells

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Chitinase is a rate-limiting and endo-splitting enzyme involved in the bio-degradation of chitin, an important component of the cuticular exoskeleton and peritrophic matrix in insects. We isolated a cDNA-encoding chitinase from the last larval integument of the cabbage moth, Mamestra brassicae (Lepidoptera; Noctuidae), cloned the ORF cDNA into E. coli to confirm its functionality, and analyzed the deduced amino acid sequence in comparison with previously described lepidopteran chitinases. M. brassicae chitinase expressed in the transformed E. coli cells with the chitinase-encoding cDNA enhanced cell proliferation to about 1.6 times of the untransformed wild type strain in a colloidal chitin-including medium with only a very limited amount of other nutrients. Compared with the wild type strain, the intracellular levels of chitin degradation derivatives, glucosamine and N-acetylglucosamine were about 7.2 and 2.3 times higher, respectively, while the extracellular chitinase activity was about 2.2 times higher in the transformed strain. The ORF of M. brassicae chitinaseencoding cDNA consisted of 1686 nucleotides (562 amino acid residues) except for the stop codon, and its deduced amino acid composition revealed a calculated molecular weight of 62.7 and theoretical pI of 5.3. The ORF was composed of N-terminal leading signal peptide (AA 1-20), catalytic domain (AA 21-392), linker region (AA 393-498), and C-terminal chitin-binding domain showing its characteristic structure as a molting fluid chitinase. In phylogenetic analysis, the enzymes from 6 noctuid species were grouped together, separately from a group of 3 bombycid and 1 tortricid enzymes, corresponding to their taxonomic relationships at both the family and genus levels.

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Section: Resultsmentioning

confidence: 76%

Section: Resultsmentioning

confidence: 98%

Section: Real-time Quantitative Reverse Transcription Pcr (Rt-pcr) Anmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Molecular Cloning and Functional Expression of Chitinase-Encoding cDNA from the Cabbage Moth, Mamestra brassicae

Paek

Park

Jeong

2012

Molecules and Cells

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Cloning, expression, and localization of a molt‐related β‐N‐acetylglucosaminidase in the spruce budworm, Choristoneura fumiferana

Zheng

Krell

Doucet

et al. 2008

Arch Insect Biochem Physiol

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A β-N-acetylglucosaminidase cDNA (Cf GlcNAcase) was cloned from the spruce budworm, Choristoneura fumiferana. Western blotting analysis of developmental Cf GlcNAcase expression revealed high levels of expression of the gene on the last day of the 5th instar larvae and the first day in the 6th instar larvae, followed by a decrease to background levels during the intermolt of the 6th instar. Cf GlcNAcase was detected again from the last day of the 6th instar to day 2 of pupal stage. Cf GlcNAcase expression was induced by tebufenozide at 24 h post treatment and remained at high levels until 72 h. Immunohistochemical localization analysis of Cf GlcNAcase indicated that Cf GlcNAcase was present in the molting fluid, epidermis, trachea, and hemolymph in prepupae during the transformation from larva to pupa. Cf GlcNAcase cDNA was expressed into a recombinant protein in bacterial and baculovirus systems and the protein expressed in the baculovirus system had a higher chitinolytic activity than in the bacterial system and appeared to be secreted. Arch. Insect Biochem. Physiol. 68:49-59, 2008.

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FUNCTIONAL ANALYSIS OF TWO CHITINASE GENES DURING THE PUPATION AND ECLOSION STAGES OF THE BEET ARMYWORM Spodoptera exigua BY RNA INTERFERENCE

Zhang

Chen

Yao

et al. 2012

Arch Insect Biochem Physiol

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Insect chitinases are a multigene family that is encoded by a rather large and diverse group of genes. The main function of chitinases is to digest the chitin contained in tissues such as the cuticles and gut lining during molting. In this study, we examined the role of a chitinase (SeChi) and a bacterial type chitinase (SeChi-h) during the pupation and eclosion stages of Spodoptera exigua. First, efficient silencing of the SeChi and SeChi-h genes through specific double-stranded RNA (dsRNA) injection led to a significant reduction in the mRNA levels of SeChi and SeChi-h. Additionally, different phenotypic defects were observed at the pupal and adult stages after injection of the SeChi and SeChi-h dsRNAs. After injecting SeChi dsRNA in the pupal stage, the cuticle of the head split open and the pupal cuticle was visible under the old larval cuticle. However, after injecting the SeChi-h dsRNA, animals died without exhibiting any special phenotypes. At the adult death stage, animals injected with dsSeChi could not shed their pupal shell completely, and their old cuticles remained attached to their head or chest. However, the main lethal phenotype was that insects did not emerge after dsSeChi-h injection. Additionally, the average survival rates of S. exigua were 52.02% and 40.38% at the pupal and adult stages, respectively, after injection with SeChi dsRNA. For the insects injected with SeChi-h dsRNA, the survival rates were 72.38% and 48.52%, respectively. These results suggest that SeChi and SeChi-h may have different biologic functions during the pupal-adult molting.

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A molt-associated chitinase cDNA from the spruce budworm, Choristoneura fumiferana

Cited by 54 publications

References 36 publications

Molecular Cloning and Functional Expression of Chitinase-Encoding cDNA from the Cabbage Moth, Mamestra brassicae

Molecular Cloning and Functional Expression of Chitinase-Encoding cDNA from the Cabbage Moth, Mamestra brassicae

Cloning, expression, and localization of a molt‐related β‐N‐acetylglucosaminidase in the spruce budworm, Choristoneura fumiferana

FUNCTIONAL ANALYSIS OF TWO CHITINASE GENES DURING THE PUPATION AND ECLOSION STAGES OF THE BEET ARMYWORM Spodoptera exigua BY RNA INTERFERENCE

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