Cloning and characterization of a gut‐specific cathepsin L from the aphid <i>Aphis gossypii</i>

Deraison, Céline; Darboux, Isabelle; Duportets, Line; Gorojankina, T.; Rahbé, Yvan; Jouanin, Lise

doi:10.1111/j.0962-1075.2004.00474.x

Cited by 71 publications

(46 citation statements)

References 53 publications

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“…Other contigs with putative functional importance for aphid host-plant interaction, including chemosensory proteins (Table 1), are related to sensing and tasting of plant compounds (Wanner et al, 2005), which have been (Cristofoletti et al, 2003;Rahbé et al, 2003;Deraison et al, 2004).…”

Section: Xenobiotic Detoxificationmentioning

confidence: 99%

Annotated expressed sequence tags and xenobiotic detoxification in the aphid Myzus persicae (Sulzer)

et al. 2007

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Aphids (Hemiptera: Aphididae) are phytophagous insects that are important agricultural pests. The enormous negative economic impacts caused by aphids worldwide are well known, and are mostly due to their high multiplication rate and the transmission of phytopathogenic viruses. Aphid management strategies mainly involve chemical treatments which are pollutants and are increasingly inefficient, since aphids have developed multiple insecticide-resistant mechanisms. Among the most economically important species is the green peach aphid Myzus persicae Sulzer (Aphididae: Macrosiphini), which is able to colonize a wide range of host plants belonging to many different families, and transmits numerous plant viruses. Because of its large prevalence, M. persicae has been the target of massive insecticide treatments; consequently, it has evolved several insecticide-resistant mechanisms. In this work, a collection of expressed genes from M. persicae is presented in order to identify putative genes involved in xenobiotic detoxification. After cDNA cloning and sequencing, 959 expressed sequence tags (EST) were annotated. Most sequences matched known genes corresponded to metabolism proteins (26%), ribosomal proteins (23%) and structural proteins (8%). Among them, several sequences corresponded to proteins putatively involved in sensing, degradation or detoxification of plant xenobiotic products.

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Section: Xenobiotic Detoxificationmentioning

confidence: 99%

Annotated expressed sequence tags and xenobiotic detoxification in the aphid Myzus persicae (Sulzer)

et al. 2007

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“…Essential amino acids are also supplied by the presence of symbionts (Douglas, 1998). However, studies have now demonstrated the presence of proteases within the gut of aphids (Cristofoletti et al, 2003(Cristofoletti et al, , 2006Deraison et al, 2004), suggesting that they are capable of digestive proteolysis. The aphid A. pisum has a midgut aminopeptidase (Rahbé et al, 1995) and a cathepsin-L-like cysteine proteinase (Cristofoletti et al, 2003).…”

Section: Discussionmentioning

confidence: 99%

“…The aphid A. pisum has a midgut aminopeptidase (Rahbé et al, 1995) and a cathepsin-L-like cysteine proteinase (Cristofoletti et al, 2003). The occurrence of a cysteine proteinase may be general among aphids since a similar enzyme was found in Brevicoryne brassicae (L.) (Silva et al, 2010) and a candidate cathepsin-L was cloned from Aphis gossypii (Glover) (Deraison et al, 2004). A cysteine proteinase inhibitor, oryzacystatin I (OC-I), has been shown to be active in M. persicae, successfully decreasing endogenous protease activity .…”

Section: Discussionmentioning

confidence: 99%

Effects of Manduca sexta allatostatin and an analogue on the peach‐potato aphid Myzus persicae (hemiptera: aphididae) and degradation by enzymes in the aphid gut

Matthews¹,

Down²,

Audsley³

2010

Arch Insect Biochem Physiol

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The oral toxicity of the C-type allatostatin, Manduca sexta allatostatin (Manse-AS) and the analogue δR³δR⁵Manse-AS, where R residues were replaced by their D-isomers, were tested against the peach-potato aphid Myzus persicae by incorporation into an artificial diet. Both peptides had significant dose-dependent effects on mortality, growth, and fecundity compared with control insects. The analogue, δR³δR⁵Manse-AS, had an estimated LC₅₀ of 0.31 µg/µl diet and was more potent than Manse-AS (estimated LC₅₀ of 0.58 µg/µl diet). At a dose of 0.35 µg δR³δR⁵Manse-AS/µl diet, 76% of the aphids were dead after 6 days and all were dead after 10 days. In comparison, three times the dose of Manse-AS was required to achieve 74% mortality after 8 days and 98% mortality after 16 days. The degradation of both peptides by extracts prepared from the gut of M. persicae was investigated. The estimated half-life of Manse-AS, when incubated with the gut extract from M. persicae, was 31 min. Degradation was due to a cathepsin L-like cysteine protease, carboxypeptidase-like activity, endoprotease activity with glutamine specificity, pyroglutamate aminopeptidase activity, and possibly trypsin-like proteases. The half-life of the δR³δR⁵ Manse-AS analogue was enhanced (73 min) with the D-isomers of R appearing to prevent cleavage around the R residues by cathepsin L-like cysteine proteases or from trypsin-like proteases. The greater stability of the analogue may explain its increased potency in M. persicae. This work demonstrates the potential use of Manse-AS and analogues, with greater resistance to enzymatic attack, in aphid control strategies.

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“…There are also considerable variations in stomach pH. Altohugh the pH in the stomach of aphids was estimated to be approximately 5.0-6.0 (Deraison et al, 2004), the pH in the midgut of S. exigua is much more alkaline with values ranging from 8 to 11 (own unpublished results). In addition, a potential reason for the different toxicity can also be the binding of the lectin to cells, its entry into the cells, intracellular routing, and degradation of the protein.…”

Section: Toxicity Of Elderberry Rip Lectin In Insectsmentioning

confidence: 98%

Entomotoxic action of Sambucus nigra agglutinin i in Acyrthosiphon pisum aphids and Spodoptera exigua caterpillars through caspase‐3‐like‐dependent apoptosis

Shahidi-Noghabi

Damme

Mahdian

et al. 2010

Arch Insect Biochem Physiol

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In this project, the toxicity and mechanism of action of the ricin-B-related lectin SNA-I from elderberry (Sambucus nigra) in the pea aphid (Acyrthosiphon pisum) and the beet armyworm (Spodoptera exigua), two important pest insects in agriculture, were studied. SNA-I is a chimeric lectin belonging to the class of ribosome-inactivating proteins and consists of an A-chain with N-glycosidase activity and a carbohydrate-binding B-chain. Incorporation of 2 mg/ml of SNA-I in the diet of neonates and adults of A. pisum caused 40-46% mortality within 2 days, while in third instars of S. exigua, the larval biomass was significantly reduced by 12% after feeding for 3 days on a diet containing 5 mg/g of SNA-I. Interestingly, extracts of the (mid)gut of treated A. pisum and S. exigua demonstrated DNA fragmentation and this was accompanied with an increase in caspase-3-like activity. The involvement of cell death or apoptosis in the entomotoxicity of SNA-I through induction of caspase-3-like activity was also confirmed by addition of the permeable caspase-3 inhibitor III in the diet, leading to a rescue of the treated aphid neonates. Finally, similar to the chimeric lectin SNA-I, the hololectin SNA-II, consisting of two carbohydrate-binding B-chains caused high mortality to neonate A. pisum aphids with an LC₅₀ of 1.59 mg/ml, suggesting that the entomotoxic action of the lectins under study mainly relies on their carbohydrate-binding activity.

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Cloning and characterization of a gut‐specific cathepsin L from the aphid Aphis gossypii

Cited by 71 publications

References 53 publications

Annotated expressed sequence tags and xenobiotic detoxification in the aphid Myzus persicae (Sulzer)

Annotated expressed sequence tags and xenobiotic detoxification in the aphid Myzus persicae (Sulzer)

Effects of Manduca sexta allatostatin and an analogue on the peach‐potato aphid Myzus persicae (hemiptera: aphididae) and degradation by enzymes in the aphid gut

Entomotoxic action of Sambucus nigra agglutinin i in Acyrthosiphon pisum aphids and Spodoptera exigua caterpillars through caspase‐3‐like‐dependent apoptosis

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