Midgut cysteine protease-inhibiting activity in Trichoplusia ni protects the peritrophic membrane from degradation by plant cysteine proteases

Li, Changyou; Song, Xiaozhao; Li, Guoxun; Wang, Ping

doi:10.1016/j.ibmb.2009.08.008

Cited by 18 publications

(9 citation statements)

References 44 publications

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“…In previous research, Mp708 showed resistance to European corn borer (Davis et al, 1989) and other insect pests of maize (Davis et al, 1988;Gill et al, 2011). These results and the likelihood of evolutionarily conserved PM functions (Bolognesi et al, 2008) suggest that upregulation of PM production and digestive enzymes is a universal component of a caterpillar's compensatory response to the presence of Mir1-CP or other cysteine proteases (Li et al, 2009) in its diet. Transcriptional regulation of MG genes may be a common means by which insects adapt to plant defenses that affect MG physiology.…”

Section: Discussionmentioning

confidence: 68%

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Maize toxin degrades peritrophic matrix proteins and stimulates compensatory transcriptome responses in fall armyworm midgut

Fescemyer

Sandoya

Gill

et al. 2013

Insect Biochemistry and Molecular Biology

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Section: Discussionmentioning

confidence: 68%

“…Lepidopterans that feed on laticiferous plants protect their PM from degradation by expressing cysteine proteaseinhibitors (Li et al, 2009). These inhibitors were not detected in the present study possibly because they were not present in the EST reference library against which sequence reads were mapped.…”

Section: Discussionmentioning

confidence: 99%

Maize toxin degrades peritrophic matrix proteins and stimulates compensatory transcriptome responses in fall armyworm midgut

Fescemyer

Sandoya

Gill

et al. 2013

Insect Biochemistry and Molecular Biology

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“…In particular, plant PIs reduce the activity of the digestive enzymes in the guts of herbivorous insects, resulting in serious developmental malformations, lethality and reduced procreation3233. Previous studies reported that plants produce more PIs with multidomains and multimeric structures, which have antinutritional effects on Spodoptera frugiperda 34.…”

Section: Discussionmentioning

confidence: 99%

Draft genome sequence of the mulberry tree Morus notabilis

et al. 2013

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Human utilization of the mulberry–silkworm interaction started at least 5,000 years ago and greatly influenced world history through the Silk Road. Complementing the silkworm genome sequence, here we describe the genome of a mulberry species Morus notabilis. In the 330-Mb genome assembly, we identify 128 Mb of repetitive sequences and 29,338 genes, 60.8% of which are supported by transcriptome sequencing. Mulberry gene sequences appear to evolve ~3 times faster than other Rosales, perhaps facilitating the species’ spread worldwide. The mulberry tree is among a few eudicots but several Rosales that have not preserved genome duplications in more than 100 million years; however, a neopolyploid series found in the mulberry tree and several others suggest that new duplications may confer benefits. Five predicted mulberry miRNAs are found in the haemolymph and silk glands of the silkworm, suggesting interactions at molecular levels in the plant–herbivore relationship. The identification and analyses of mulberry genes involved in diversifying selection, resistance and protease inhibitor expressed in the laticifers will accelerate the improvement of mulberry plants.

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“…However, expression of V-CATH in transgenic tobacco plants was found to retard the growth of Helicoverpa armigera (Old World bollworm) larvae that fed on the plants, suggesting that this cysteine protease may also damage or disrupt the PM. While enhancin metalloproteases and a variety of cysteine proteases can degrade PM proteins, serine proteases do not appear to be capable of degrading PM proteins in in vitro assays [53,54]. In a study testing the oral toxicity of five different proteases to pea aphids ( Acyrthosiphon pisum ) when included as part of an artificial diet, trypsin was the second most toxic protease, with an IC 50 of 22 μg/mL [55].…”

Section: Proteases With Toxicity Towards Insectsmentioning

confidence: 99%

Proteases as Insecticidal Agents

Harrison

Bonning

2010

Toxins

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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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Midgut cysteine protease-inhibiting activity in Trichoplusia ni protects the peritrophic membrane from degradation by plant cysteine proteases

Cited by 18 publications

References 44 publications

Maize toxin degrades peritrophic matrix proteins and stimulates compensatory transcriptome responses in fall armyworm midgut

Maize toxin degrades peritrophic matrix proteins and stimulates compensatory transcriptome responses in fall armyworm midgut

Draft genome sequence of the mulberry tree Morus notabilis

Proteases as Insecticidal Agents

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