The impact of ingested potato type II inhibitors on the production of the major serine proteases in the gut of Helicoverpa armigera

Stevens, J. A.; Dunse, Kerry; Guarino, Rosemary F.; Barbeta, Barbara L.; Evans, Shelley; West, Jenny; Anderson, Marilyn A.

doi:10.1016/j.ibmb.2012.11.006

Cited by 28 publications

(22 citation statements)

References 39 publications

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“…Stevens et al. () also observed the excretion of trypsin and chymotrypsin in the frass of H. armigera larvae fed on different amounts of potato type II protease inhibitor from Nicotiana alata Link & Otto (NaPI). These authors suggested that this was due to the binding of the inhibitor to the midgut proteases and subsequent prevention of the re‐absorption of the enzymes from the endoperitrophic space into the ectoperitrophic space.…”

Section: Discussionmentioning

confidence: 97%

“…However, despite increasing chymotrypsin-like activity, IVTI-fed larvae were unable to degrade BSA in vitro. The increase in energy expenditure needed for chymotrypsin synthesis may lead to a depletion of essential sulfur-containing amino acids, affecting insect growth and development (Broadway & Duffey, 1986;Stevens et al, 2013).…”

Section: Discussionmentioning

confidence: 99%

“…The ingestion of PIs by insects leads to the deregulation of the insect's digestive proteases. The reactive site of the PI interacts with the active site of its target enzyme, forming a stable complex and consequently blocking the enzyme's activity, in turn compromising the insect's normal physiology and affecting its development (Stevens et al, 2013;Oliveira et al, 2014;Abd El-latif, 2015;Jamal et al, 2015). When the serine PIs are ingested by phytophagous insects they interact with proteolytic enzymes in their digestive tract, including the trypsin and chymotrypsin-like enzymes (Jamal et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

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Inga vera trypsin inhibitor interferes in the proteolytic activity and nutritional physiology of Ephestia kuehniella larvae

Bezerra

Oliveira

Macedo

2017

Entomologia Exp Applicata

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Plant peptidase inhibitors provide plants with a defense strategy to inhibit insect digestive enzymes and have been studied as an alternative strategy for pest control as they interfere in normal insect physiology. We evaluated the effects of ingestion of the trypsin inhibitor from Inga vera Willd. (Fabaceae) seeds on the nutritional and digestive physiology of Ephestia kuehniella (Zeller) (Lepidoptera: Pyralidae) larvae. Inga vera trypsin inhibitor (IVTI) reduced the efficiency of the conversion of ingested and digested food in these larvae and increased the metabolic cost, causing an anti‐nutritional effect. In both short‐ and long‐term bioassays, the ingestion of IVTI inactivated most of the insect's trypsin activity, but increased chymotrypsin activity as a compensatory response by the insect; however, protein digestion continued to be partially blocked. Consequently, chymotrypsin‐like enzymes, which were over‐produced in the gut, were excreted more into the frass of IVTI‐fed larvae. As such, the resistance of IVTI to hydrolysis by insect midgut proteases resulted in detrimental effects to larvae. These data provide support for the use of IVTI as a biotechnological tool for pest control.

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Section: Discussionmentioning

confidence: 97%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Inga vera trypsin inhibitor interferes in the proteolytic activity and nutritional physiology of Ephestia kuehniella larvae

Bezerra

Oliveira

Macedo

2017

Entomologia Exp Applicata

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“…Peptides (as quantified above) were incubated at various concentrations (range from 2.5 nM to 7.5 mM) with 5 mg of Helicoverpa armigera fourth instar total gut extract prepared as described by Stevens et al (2013). Trypsin activity was measured using the commercially available substrate Benzoyl-FVR-pNA (Sigma-Aldrich), and chymotrypsin activity was measured using Succ-AAPFpNA (Sigma-Aldrich).…”

Section: Insect Trypsin and Chymotrypsin Inhibitory Assaysmentioning

confidence: 99%

Evolutionary Origins of a Bioactive Peptide Buried within Preproalbumin

et al. 2014

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The de novo evolution of proteins is now considered a frequented route for biological innovation, but the genetic and biochemical processes that lead to each newly created protein are often poorly documented. The common sunflower (Helianthus annuus) contains the unusual gene PawS1 (Preproalbumin with SFTI-1) that encodes a precursor for seed storage albumin; however, in a region usually discarded during albumin maturation, its sequence is matured into SFTI-1, a protease-inhibiting cyclic peptide with a motif homologous to unrelated inhibitors from legumes, cereals, and frogs. To understand how PawS1 acquired this additional peptide with novel biochemical functionality, we cloned PawS1 genes and showed that this dual destiny is over 18 million years old. This new family of mostly backbone-cyclic peptides is structurally diverse, but the protease-inhibitory motif was restricted to peptides from sunflower and close relatives from its subtribe. We describe a widely distributed, potential evolutionary intermediate PawS-Like1 (PawL1), which is matured into storage albumin, but makes no stable peptide despite possessing residues essential for processing and cyclization from within PawS1. Using sequences we cloned, we retrodict the likely stepwise creation of PawS1's additional destiny within a simple albumin precursor. We propose that relaxed selection enabled SFTI-1 to evolve its inhibitor function by converging upon a successful sequence and structure.

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“…However, Stevens et al (2013) proposed that H. armigera larvae feeding on a diet 471 containing NaPI do not overproduce trypsins or chymotrypsins, but excessively excrete them 472 in their frass. Reduced total protease activity was mirrored by reduced trypsin activity in 473 SKTI diet fed larvae compared to control larvae, confirming the fact that SKTI-sensitive 474 trypsin activity is a major fraction of the total protease activity in H. armigera.…”

Section: A C C E P T E D Accepted Manuscriptmentioning

confidence: 99%

Adaptive regulation of digestive serine proteases in the larval midgut of Helicoverpa armigera in response to a plant protease inhibitor

Kuwar

Pauchet

Vogel

et al. 2015

Insect Biochemistry and Molecular Biology

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The impact of ingested potato type II inhibitors on the production of the major serine proteases in the gut of Helicoverpa armigera

Cited by 28 publications

References 39 publications

Inga vera trypsin inhibitor interferes in the proteolytic activity and nutritional physiology of Ephestia kuehniella larvae

Inga vera trypsin inhibitor interferes in the proteolytic activity and nutritional physiology of Ephestia kuehniella larvae

Evolutionary Origins of a Bioactive Peptide Buried within Preproalbumin

Adaptive regulation of digestive serine proteases in the larval midgut of Helicoverpa armigera in response to a plant protease inhibitor

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