Chitin deacetylase family genes in the brown planthopper, <i><scp>N</scp>ilaparvata lugens</i> (<scp>H</scp>emiptera: <scp>D</scp>elphacidae)

X, Yu; Pan, Peng-Lu; Ye, Y.-X.; Yu, Bing; Zhang, Chuan‐Xi

doi:10.1111/imb.12113

Cited by 89 publications

(120 citation statements)

References 22 publications

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“…The N. lugens insects used in this study were obtained from local rice fields at the Huajiachi campus, Zhejiang University, Hangzhou, China, and reared on fresh rice seedlings (Taichung Native 1) under standard laboratory conditions (temperature: 25 ± 1 °C; relative humidity: 60–70%; photoperiod: 16 h/8 h, light/dark), as described previously (Xi et al ., ).…”

Section: Methodsmentioning

confidence: 99%

The β‐N‐acetylhexosaminidase gene family in the brown planthopper, Nilaparvata lugens

Yang

Pan

Zhang

2015

Insect Molecular Biology

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β-N-Acetylhexosaminidases (HEXs) are enzymes that can degrade the chitin oligosaccharides that are produced by the activity of chitinases on chitin in insects. Using bioinformatic methods based on genome and transcriptome databases, 11 β-N-acetylhexosaminidase genes (NlHexs) in Nilaparvata lugens were identified and characterized. Phylogenetic analysis revealed a six-grouped tree topology. The O-Linked N-acetylglucosaminidase (O-GlcNAcase) group includes NlHex11, which harbours a catalytic domain that differs from that of the other 10 NlHexs. Observations of the expression of NlHexs during different developmental stages revealed that NlHex4 is expressed with periodicity during moulting. Although the tissue-specific expression patterns of most NlHexs were nonspecific, NlHex4 was found to be expressed mainly in the female reproductive system as well as in the integument. RNA interference (RNAi) demonstrated failure to shed the old cuticle only in the nymphs treated with double-stranded RNA (dsRNA) targeting NlHex4, and these nymphs eventually died; no observable morphological abnormalities were found in insects treated with dsRNAs targeting the other 10 NlHexs. Based on this study and our previous analyses, a '5 + 1 + 3' pattern of chitinolytic enzymes is proposed, in which five chitinases, one NlHEX and three chitin deacetylases are required for moulting in N. lugens. A better understanding of chitin metabolism in the hemimetabolous insect, N. lugens, would be achieved by considering three chitinolytic enzyme families: chitinase, chitin deacetylase and β-N-acetylhexosaminidase.

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Section: Methodsmentioning

confidence: 99%

The β‐N‐acetylhexosaminidase gene family in the brown planthopper, Nilaparvata lugens

Yang

Pan

Zhang

2015

Insect Molecular Biology

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“…(), mutation in vermiform ( verm , CDA2 ) in the common fruit fly Drosophila melanogaster leads to elongated and tortuous tracheal tubes (Luschnig et al ., ; Wang et al ., ) and results in disorganized larval cuticle (Gangishetti et al ., ). Moreover, RNAi of CDA2 in the eastern spruce budworm Choristoneura fumiferana (Quan et al ., ), the brown planthopper Nilaparvata lugens (Xi et al ., ), and the red flour beetle Tribolium castaneum (Arakane et al ., ) causes molting failure. Despite these reports, however, current knowledge on the physiological roles of insect CDA2s is rather limited (Yu et al ., ).…”

Section: Introductionmentioning

confidence: 99%

Silencing chitin deacetylase 2 impairs larval–pupal and pupal–adult molts in Leptinotarsa decemlineata

Chen

Wang

et al. 2018

Insect Molecular Biology

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Insect chitin deacetylases (CDAs) are carbohydrate esterases that catalyze N-deacetylation of chitin to generate chitosan, a process essential for chitin organization and compactness during the formation of extracellular chitinous structure. Here we identified two CDA2 splice variants (LdCDA2a and LdCDA2b) in Leptinotarsa decemlineata. Both splices were abundantly expressed in larval foregut, rectum, and epidermis; their levels peaked immediately before ecdysis within each instar. In vivo results revealed that the two isoforms transcriptionally responded, positively and negatively respectively, to 20-hydroxyecdysone and juvenile hormone signaling pathways. RNA interference (RNAi)-aided knockdown of the two LdCDA2 variants (hereafter LdCDA2) or LdCDA2b, rather than LdCDA2a, resulted in three negative effects. First, foliage consumption was significantly reduced, larval developing period was lengthened, and larval growth was retarded. Second, chitin contents were reduced, whereas glucose, trehalose, and glycogen contents were increased in the LdCDA2 and LdCDA2b RNAi larvae. Third, approximately 20% of LdCDA2 and LdCDA2b RNAi larvae were trapped within the exuviae and finally died. About 60% of the abnormal pupae died as pharate adults. Around 20% of the RNAi pupae emerged as deformed adults, with small size and wrinkled wings. These adults eventually died within 1 week after molting. Our results reveal that knockdown of CDA2 affects chitin accumulation. Consequently, LdCDA2 may be a potential target for control of L. decemlineata larvae.

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“…CDAs are broadly conserved, known to occur not only in all fungi (Ruiz‐Herrera & Ortiz‐Castellanos, 2010) but also in insects, where they have a number of developmental roles, including in tracheal development and moulting (Arakane et al . , 2009; Luschnig, Batz, Armbruster, & Krasnow, 2006; Wang, Jayaram, et al, 2006b; Xi, Pan, Ye, Yu, & Zhang, 2014). Considering the relative chemical and physical properties of chitin and chitosan, we hypothesized that chitin deacetylation could also have key roles in fungal development.…”

Section: Introductionmentioning

confidence: 99%

Investigating chitin deacetylation and chitosan hydrolysis during vegetative growth in Magnaporthe oryzae

Geoghegan

Gurr

2017

Cellular Microbiology

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SummaryChitin deacetylation results in the formation of chitosan, a polymer of β1,4‐linked glucosamine. Chitosan is known to have important functions in the cell walls of a number of fungal species, but its role during hyphal growth has not yet been investigated. In this study, we have characterized the role of chitin deacetylation during vegetative hyphal growth in the filamentous phytopathogen Magnaporthe oryzae. We found that chitosan localizes to the septa and lateral cell walls of vegetative hyphae and identified 2 chitin deacetylases expressed during vegetative growth—CDA1 and CDA4. Deletion strains and fluorescent protein fusions demonstrated that CDA1 is necessary for chitin deacetylation in the septa and lateral cell walls of mature hyphae in colony interiors, whereas CDA4 deacetylates chitin in the hyphae at colony margins. However, although the Δcda1 strain was more resistant to cell wall hydrolysis, growth and pathogenic development were otherwise unaffected in the deletion strains. The role of chitosan hydrolysis was also investigated. A single gene encoding a putative chitosanase (CSN) was discovered in M. oryzae and found to be expressed during vegetative growth. However, chitosan localization, vegetative growth, and pathogenic development were unaffected in a CSN deletion strain, rendering the role of this enzyme unclear.

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Chitin deacetylase family genes in the brown planthopper, Nilaparvata lugens (Hemiptera: Delphacidae)

Cited by 89 publications

References 22 publications

The β‐N‐acetylhexosaminidase gene family in the brown planthopper, Nilaparvata lugens

The β‐N‐acetylhexosaminidase gene family in the brown planthopper, Nilaparvata lugens

Silencing chitin deacetylase 2 impairs larval–pupal and pupal–adult molts in Leptinotarsa decemlineata

Investigating chitin deacetylation and chitosan hydrolysis during vegetative growth in Magnaporthe oryzae

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