Cysteine digestive peptidases function as post-glutamine cleaving enzymes in tenebrionid stored-product pests

Goptar, Irina A.; Semashko, Tatiana A.; Danilenko, S.A.; Lysogorskaya, E. N.; Oksenoit, E. S.; Zhuzhikov, D. P.; Belozersky, M. A.; Dunaevsky, Ya. E.; Oppert, Brenda; Filippova, I. Yu.; Elpidina, Elena N.

doi:10.1016/j.cbpb.2011.10.005

Cited by 40 publications

(36 citation statements)

References 33 publications

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“…The evolution toward a cysteine peptidase-based digestive system in T. castaneum and presumably other tenebrionids has resulted in numerous and specialized cysteine peptidases that efficiently digest cereal proteins that have abundant glutamine residues (Goptar et al, 2012). Enhanced expression of cysteine peptidases in the anterior midgut protects serine peptidases in the posterior midgut from cereal inhibitors (Vinokurov et al, 2009).…”

Section: Discussionmentioning

confidence: 99%

“…Reliance on cysteine peptidase activity in the anterior midgut of tenebrionid larvae is probably an adaptation to degrade inhibitors and protect serine peptidases in the posterior midgut (Prabhakar et al, 2007;Oppert et al, 2010). Some cysteine peptidases also have become specialized for efficient digestion of cereal proteins (Vinokurov et al, 2009;Goptar et al, 2012;Martynov et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

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RNA interference and dietary inhibitors induce a similar compensation response in Tribolium castaneum larvae

Perkin

Elpidina

Oppert

2016

Insect Molecular Biology

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Tribolium castaneum is a major agriculture pest damaging stored grains and cereal products. The T. castaneum genome contains 26 cysteine peptidase genes, mostly cathepsins L and B, and seven have a major role in digestion. We targeted the expression of the most highly expressed cathepsin L gene on chromosome 10, TC011001, by RNA interference (RNAi), using double-stranded RNA (dsRNA) constructs of different regions of the gene (3', middle, 5' and entire coding regions). RNA sequencing and quantitation (RNA-seq) was used to evaluate knockdown and specificity amongst the treatments. Overall, target gene expression decreased in all treatment groups, but was more severe and specific in dsRNA targeting the 3' and entire coding regions, encoding the proteolytic active site in the enzyme. Additional cysteine cathepsin genes also were down-regulated (off-target effects), but some were up-regulated in response to RNAi treatment. Notably, some serine peptidase genes were increased in expression, especially in dsRNA targeting 5' and middle regions, and the response was similar to the effects of dietary cysteine protease inhibitors. We manually annotated these serine peptidase genes to gain insight into function and relevance to the RNAi study. The data indicate that T. castaneum larvae compensate for the loss of digestive peptidase activity in the larval gut, regardless of the mechanism of disruption.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

RNA interference and dietary inhibitors induce a similar compensation response in Tribolium castaneum larvae

Perkin

Elpidina

Oppert

2016

Insect Molecular Biology

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“…For example, digestive cysteine cathepsins in T. castaneum larvae became important components of adaptive responses in overcoming the effect of cereal protease inhibitors [73]. In T. castaneum and the related tenebrionid, Tenebrio molitor, large expansions of genes encoding cysteine cathepsins were driven not only by protection against inhibitors, but also by more efficient digestion of complex proteins in grains [74][75][76].…”

Section: Cysteine Peptidases From the Papain C1 Familymentioning

confidence: 99%

Brown marmorated stink bug, Halyomorpha halys (Stål), genome: putative underpinnings of polyphagy, insecticide resistance potential and biology of a top worldwide pest

Sparks¹,

Bansal

Benoit

et al. 2020

BMC Genomics

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Background: Halyomorpha halys (Stål), the brown marmorated stink bug, is a highly invasive insect species due in part to its exceptionally high levels of polyphagy. This species is also a nuisance due to overwintering in humanmade structures. It has caused significant agricultural losses in recent years along the Atlantic seaboard of North America and in continental Europe. Genomic resources will assist with determining the molecular basis for this species' feeding and habitat traits, defining potential targets for pest management strategies.

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“…Thus, it has been proposed that exogenous enzymes can be employed for additional enzyme supplement therapy to promote the complete digestion of cereal proteins, and thus destroy T-cell gluten epitopes, in particular [129,130]. A number of peptidases possessing glutenase activities were isolated from germinating cereals ( Hordeum vulgare L., Triticum aestivum L.), bacteria ( Flavobacterium meningosepticum , Sphingomonas capsulate , Myxococcus xanthus ), fungi ( Aspergillus niger , Aspergillus oryzae ), and stored-product pest yellow mealworm ( Tenebrio molitor ) [131,132,133,134,135]. One of them is ALV003 enzyme—modified recombinant EP-B2 enzyme from barley, and prolyl endopeptidase from bacteria Sphingomonas capsulate —was shown to be effective in vitro and in vivo, non-toxic and without allergic reactions [136,137].…”

Section: Gluten Detoxification Strategiesmentioning

confidence: 99%

Properties of Gluten Intolerance: Gluten Structure, Evolution, Pathogenicity and Detoxification Capabilities

2016

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Theterm gluten intolerance may refer to three types of human disorders: autoimmune celiac disease (CD), allergy to wheat and non-celiac gluten sensitivity (NCGS). Gluten is a mixture of prolamin proteins present mostly in wheat, but also in barley, rye and oat. Gluten can be subdivided into three major groups: S-rich, S-poor and high molecular weight proteins. Prolamins within the groups possess similar structures and properties. All gluten proteins are evolutionarily connected and share the same ancestral origin. Gluten proteins are highly resistant to hydrolysis mediated by proteases of the human gastrointestinal tract. It results in emergence of pathogenic peptides, which cause CD and allergy in genetically predisposed people. There is a hierarchy of peptide toxicity and peptide recognition by T cells. Nowadays, there are several ways to detoxify gluten peptides: the most common is gluten-free diet (GFD), which has proved its effectiveness; prevention programs, enzymatic therapy, correction of gluten pathogenicity pathways and genetically modified grains with reduced immunotoxicity. A deep understanding of gluten intolerance underlying mechanisms and detailed knowledge of gluten properties may lead to the emergence of novel effective approaches for treatment of gluten-related disorders.

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Cysteine digestive peptidases function as post-glutamine cleaving enzymes in tenebrionid stored-product pests

Cited by 40 publications

References 33 publications

RNA interference and dietary inhibitors induce a similar compensation response in Tribolium castaneum larvae

RNA interference and dietary inhibitors induce a similar compensation response in Tribolium castaneum larvae

Brown marmorated stink bug, Halyomorpha halys (Stål), genome: putative underpinnings of polyphagy, insecticide resistance potential and biology of a top worldwide pest

Properties of Gluten Intolerance: Gluten Structure, Evolution, Pathogenicity and Detoxification Capabilities

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