Amylase gene expression patterns in Helicoverpa armigera upon feeding on a range of host plants

Kotkar, Hemlata M; Bhide, Amey J.; Gupta, Vidya S.; Giri, Ashok P.

doi:10.1016/j.gene.2012.04.010

Cited by 20 publications

(20 citation statements)

References 38 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The gel was overlaid onto X-ray film (Fujifilm, India) for 5-10 min before subjecting it to staining with Ezee blue gel stainer (Genei-Merk, India) and / or coomassie brilliant blue R-250 staining. Since some A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT 8 of the α-AIs are resistant to trypsin, same gel can also be processed for α-AI zymography after GXCP. The apparent molecular masses of the separated α-AIs were estimated using medium range molecular weight standards (Genei-Merk, India) in 12% denaturing SDS-PAGE.…”

Section: Visualization Of Bifunctional Nature and Diversity Of Ccaismentioning

confidence: 99%

A bifunctional α-amylase/trypsin inhibitor from pigeonpea seeds: Purification, biochemical characterization and its bio-efficacy against Helicoverpa armigera

Gadge

Wagh

Shaikh

et al. 2015

Pesticide Biochemistry and Physiology

View full text Add to dashboard Cite

Section: Visualization Of Bifunctional Nature and Diversity Of Ccaismentioning

confidence: 99%

A bifunctional α-amylase/trypsin inhibitor from pigeonpea seeds: Purification, biochemical characterization and its bio-efficacy against Helicoverpa armigera

Gadge

Wagh

Shaikh

et al. 2015

Pesticide Biochemistry and Physiology

View full text Add to dashboard Cite

“…Moreover, they also induce several novel inhibitor‐resistant/degrading proteases (Jongsma et al ., ; Bown et al ., , ; Broadway, ; Gatehouse et al ., ; Jongsma & Bolter, ; Wu et al ., ; Giri et al ., ; Mazumdar‐Leighton & Broadway, , b; Zavala et al ., ; Dunse et al ., , b). Previous studies have indicated that the insects possess the strength to modify gut protease, amylase and lipase expression in accordance with both natural and PI‐containing diets (Harsulkar et al ., ; Patankar et al ., ; Chougule et al ., ; Tamhane et al ., ; Kotkar et al ., , ; Sarate et al ., ). Further exploration is required to determine how or whether the sensitivity of H. armigera protease complements plant defence molecules.…”

Section: Introductionmentioning

confidence: 98%

Differential protease activity augments polyphagy in Helicoverpa armigera

Chikate

Tamhane

Joshi

et al. 2013

Insect Molecular Biology

View full text Add to dashboard Cite

Helicoverpa armigera (Lepidoptera: Noctuidae) and other polyphagous agricultural pests are extending their plant host range and emerging as serious agents in restraining crop productivity. Dynamic regulation, coupled with a diversity of digestive and detoxifying enzymes, play a crucial role in the adaptation of polyphagous insects. To investigate the functional intricacy of serine proteases in the development and polyphagy of H. armigera, we profiled the expression of eight trypsin-like and four chymotrypsin-like phylogenetically diverse mRNAs from different life stages of H. armigera reared on nutritionally distinct host plants. These analyses revealed diet- and stage-specific protease expression patterns. The trypsins expressed showed structural variations, which might result in differential substrate specificity and interaction with inhibitors. Protease profiles in the presence of inhibitors and their mass spectrometric analyses revealed insight into their differential activity. These findings emphasize the differential expression of serine proteases and their consequences for digestive physiology in promoting polyphagy in H. armigera.

show abstract

“…First instar of H. armigera may have limited ability to adjust for discrepancy in macronutrient intake, possibly as a result of low amylase but not protease activity in the first instar (Kotkar et al . ), limiting their ability to process carbohydrates of any ratio and explaining their preferred location on the protein‐rich block. Later instars of H. armigera can vary the expression of key protease, lipase and amylase enzymes depending on host plant, and this may be an underlying physiological mechanism that is coupled with feeding behaviour to adjust feeding between diets with different macronutrient constituents (Sarate et al .…”

Section: Discussionmentioning

confidence: 99%

Life history traits of a key agricultural pest, Helicoverpa armigera (Lepidoptera: Noctuidae): are laboratory settings appropriate?

2020

View full text Add to dashboard Cite

Helicoverpa armigera is intensively researched in laboratory settings, yet developmental rates can vary considerably even under controlled conditions. Here, dietary choice and light spectra were tested as possible factors influencing this variability, a range of fitness indicators were collected and dietary choice behaviour in early instars was observed. We show that early instars of H. armigera exhibited self‐selection of nutrient intake, a novel finding. Larvae given a choice between two artificial diets varying in macronutrient ratios were heavier, exhibited a higher relative growth rate, shorter developmental time and longer eclosion time compared with larvae reared on a single diet. Wing size relative to body mass was higher for larvae on extreme no choice treatments and smallest for those on the choice diets, indicating a potential adaptation to escape poor nutrient landscapes. Light spectra had an effect on the size of pupae, with H. armigera reared under white LED light having larger pupae than those reared under fluorescent white light. Larvae reared under LED light took longer to emerge from pupation. Giving larvae a choice of diets with a range of nutrients may reduce developmental variability rather than assuming that one diets suits all.

show abstract

Amylase gene expression patterns in Helicoverpa armigera upon feeding on a range of host plants

Cited by 20 publications

References 38 publications

A bifunctional α-amylase/trypsin inhibitor from pigeonpea seeds: Purification, biochemical characterization and its bio-efficacy against Helicoverpa armigera

A bifunctional α-amylase/trypsin inhibitor from pigeonpea seeds: Purification, biochemical characterization and its bio-efficacy against Helicoverpa armigera

Differential protease activity augments polyphagy in Helicoverpa armigera

Life history traits of a key agricultural pest, Helicoverpa armigera (Lepidoptera: Noctuidae): are laboratory settings appropriate?

Contact Info

Product

Resources

About