Effect of ace inhibitors and TMOF on growth, development, and trypsin activity of larval <i>Spodoptera littoralis</i>

Lemeire, Els; Borovsky, Dov; Camp, John Van; Smagghe, Guy

doi:10.1002/arch.20270

Cited by 9 publications

(6 citation statements)

References 30 publications

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“…In a recent study on Spodoptera littoralis larvae, the presence of Aea-TMOF receptors on the basolateral membrane of midgut cells has been hypothesized (Lemeire et al, 2008). The effect of ingested and injected Aea-TMOF on trypsin biosynthesis (Nauen et al, 2001) and on the growth of H. virescens larvae (Tortiglione et al, 2002;2003) also suggests the presence of a TMOF-like hormone in Lepidoptera, and, therefore, of receptors similar to those identified in mosquitoes.…”

Section: Discussionmentioning

confidence: 99%

A viral chitinase enhances oral activity of TMOF

Fiandra

Terracciano

Fanti

et al. 2010

Insect Biochemistry and Molecular Biology

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In this study we investigate the combined effect on Heliothis virescens (Lepidoptera, Noctuidae) larvae of Aedes aegypti-Trypsin Modulating Oostatic Factor (Aea-TMOF), a peptide that inhibits trypsin synthesis by the gut, impairing insect digestive function, and Autographa californica nucleopolyhedrovirus Chitinase A (AcMNPV ChiA), an enzyme that is able to alter the permeability of the peritrophic membrane (PM). Aea-TMOF and AcMNPV ChiA were provided to the larvae by administering transgenic tobacco plants, co-expressing both molecules. Experimental larvae feeding on these plants, compared to those alimented on plants expressing only one of the two molecules considered, showed significantly stronger negative effects on growth rate, developmental time and mortality. The impact of AcMNPV ChiA on the PM of H. virescens larvae, measured as increased permeability to molecules, was evident after five days of feeding on transgenic plants expressing ChiA. This result was confirmed by in vitro treatment of PM with recombinant ChiA, extracted from the transgenic plants used for the feeding experiments. Collectively, these data indicate the occurrence of a positive interaction between the two transgenes concurrently expressed in the same plant. The hydrolytic activity of ChiA on the PM of tobacco budworm larvae enhances the permeation of TMOF molecules to the ectoperitrophic space, and its subsequent absorption. The permeation through the paracellular route of Aea-TMOF resulted in a spotted accumulation on the basolateral domain of enterocytes, which suggests the occurrence of a receptor on the gut side facing the haemocoel. The binding of the peptide, permeating at increased rates due to the ChiA activity, is considered responsible for the enhanced insecticide activity of the transgenic plants expressing both molecules. These data corroborate the idea that ChiA can be effectively used as gut permeation enhancer in oral delivery strategies of bioinsecticides targeting haemocoelic receptors. Dear Rene,We have revised the manuscript as requested. Below are the reviewers comments and for each issue raised our remedial action or an explanation to address their concerns is reported in bold.I think that this version is certainly improved, and we will be glad to consider any further suggestion you may have. All the best, FrancoReviewer #1: Fiandra et al.In this manuscript Fiandra et al present some interesting data on apparent enhancement of TMOF action by chitinase. Overall, this is a sound study that will be improved with the following modifications:1. What is the mechanism of action of TMOF? This should be introduced upfront. The action of TMOF in inhibiting trypsin synthesis and impeding larval digestive processes is key to the logic behind these experiments. Not until page 16 is this information provided for the reader! This information should actually be included in the abstract. Clearly introduce TMOF.The information requested has been added in the manuscript (Abstract and Introduction). Page 4What is the size o...

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Section: Discussionmentioning

confidence: 99%

A viral chitinase enhances oral activity of TMOF

Fiandra

Terracciano

Fanti

et al. 2010

Insect Biochemistry and Molecular Biology

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“…A separate review in this volume by Rodou and colleagues provides an in-depth overview of the insecticidal proteases of the bacterium Photorhabdus luminescens . Related to the use of proteolytic enzymes as insecticidal agents is exploitation of the insecticidal impact of the lack of proteases, such as plant expression of inhibitors of herbivore gut proteases [21], and the use of insect-derived, trypsin-modulating oostatic factor that inhibits trypsin biosynthesis in the insect gut [22,23]. The insecticidal effects of protease inhibition will not be considered in the current review.…”

Section: Toxic Proteins As Insecticidal Agentsmentioning

confidence: 99%

Proteases as Insecticidal Agents

Harrison

Bonning

2010

Toxins

100

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Proteases from a variety of sources (viruses, bacteria, fungi, plants, and insects) have toxicity towards insects. Some of these insecticidal proteases evolved as venom components, herbivore resistance factors, or microbial pathogenicity factors, while other proteases play roles in insect development or digestion, but exert an insecticidal effect when over-expressed from genetically engineered plants or microbial pathogens. Many of these proteases are cysteine proteases, although insect-toxic metalloproteases and serine proteases have also been examined. The sites of protease toxic activity range from the insect midgut to the hemocoel (body cavity) to the cuticle. This review discusses these insecticidal proteases along with their evaluation and use as potential pesticides.

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“…Nevertheless, ACE inhibitors can be acutely toxic to insects, which contrasts with their life-span extending properties in rodents37 and the nematode, Caenorhabditis elegans 38. They have been useful in confirming important roles for ACE in reproduction, growth and development in several insect species30343539. In the mosquito Anopheles stephensi , females fed with ACE inhibitors in the blood meal or females mated with males supplied with ACE inhibitors in their sugar diet, lay significantly fewer eggs than normal323540.…”

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confidence: 99%

The toxicity of angiotensin converting enzyme inhibitors to larvae of the disease vectors Aedes aegypti and Anopheles gambiae

Hasan

Williams

Ismail

et al. 2017

Sci Rep

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The control of mosquitoes is threatened by the appearance of insecticide resistance and therefore new control chemicals are urgently required. Here we show that inhibitors of mosquito peptidyl dipeptidase, a peptidase related to mammalian angiotensin-converting enzyme (ACE), are insecticidal to larvae of the mosquitoes, Aedes aegypti and Anopheles gambiae. ACE inhibitors (captopril, fosinopril and fosinoprilat) and two peptides (trypsin-modulating oostatic factor/TMOF and a bradykinin-potentiating peptide, BPP-12b) were all inhibitors of the larval ACE activity of both mosquitoes. Two inhibitors, captopril and fosinopril (a pro-drug ester of fosinoprilat), were tested for larvicidal activity. Within 24 h captopril had killed >90% of the early instars of both species with 3rd instars showing greater resistance. Mortality was also high within 24 h of exposure of 1st, 2nd and 3rd instars of An. gambiae to fosinopril. Fosinopril was also toxic to Ae. aegypti larvae, although the 1st instars appeared to be less susceptible to this pro-drug even after 72 h exposure. Homology models of the larval An. gambiae ACE proteins (AnoACE2 and AnoACE3) reveal structural differences compared to human ACE, suggesting that structure-based drug design offers a fruitful approach to the development of selective inhibitors of mosquito ACE enzymes as novel larvicides.

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Effect of ace inhibitors and TMOF on growth, development, and trypsin activity of larval Spodoptera littoralis

Cited by 9 publications

References 30 publications

A viral chitinase enhances oral activity of TMOF

A viral chitinase enhances oral activity of TMOF

Proteases as Insecticidal Agents

The toxicity of angiotensin converting enzyme inhibitors to larvae of the disease vectors Aedes aegypti and Anopheles gambiae

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