Interaction of <i>Allium sativum</i> leaf agglutinin with midgut brush border membrane vesicles proteins and its stability in <i>Helicoverpa armigera</i>

Singh

2012

Protein J

Garlic (Allium sativum) lectins are promising candidate molecules for the protection against chewing (lepidopteran) as well as sap sucking (homopteran) insect pests. Molecular mechanism of toxicity and interaction of lectins with midgut receptor proteins has been described in many reports. Lectins show its effect right from sensory receptors of mouth parts by disrupting the membrane integrity and food detection ability. Subsequently, enter into the gut lumen and interact with midgut glycosylated proteins like alkaline phosphatase (ALP), aminopeptidase-N (APN), cadherin-like proteins, polycalins, sucrase, symbionin and others. These proteins play critical role in life cycle of insect directly or indirectly. Lectins interfere with the activity of these proteins and causes physiological disorders leading to the death of insects. Lectins further transported across the insect gut, accumulated in various body parts (like haemolymph and ovary) and interact with intracellular proteins like symbionin and cytochrome p450. Binding with cytochrome p450 (which involve in ecdysone synthesis) might interfere in the development of insects, which results in growth retardation and pre-mature death.

Section: Cadherin Like Proteinmentioning

confidence: 63%

Section: Putative Receptors Of Garlic Lectins In the Midgut Of Insectsmentioning

confidence: 99%

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Receptors of Garlic (Allium sativum) Lectins and Their Role in Insecticidal Action

Singh

2012

Protein J

“…The bound proteins were eluted with unbuffered Na 2 CO 3 (100 mM, pH. 12.0) [29] and used for further analysis.…”

Section: Sds-page Analysismentioning

confidence: 99%

Interaction of Salivary and Midgut Proteins of Helicoverpa armigera with Soybean Trypsin Inhibitor

Chandrashekar

2012

Protein J

Self Cite

Feeding of Helicoverpa armigera larvae on semi-synthetic diet containing Soybean trypsin inhibitor (STI) resulted in disappearance of STI sensitive protease in salivary and midgut protease extract. This might be due to in situ inhibition by dietary STI. STI was largely degraded within 1 h of incubation with total salivary protease (1:1). Degradation was relatively low in midgut proteases. STI interacting proteins were isolated from saliva and midgut extracts of larvae fed on STI supplemented diet using affinity column. Most of the isolated proteins showed caseinolytic activity in zymogram. Denovo sequencing data of seven different peptides selected from trypsin digested total protein showed similarity to chymotrypsinogen, serine protease, aminopeptidase N, peroxidase, hypothetical protein and muscle specific protein.

“…Pellet was resuspended in half of the original volume of MET and MgCl 2 and above steps were repeated. The final pellet was solubilised in phosphate buffer saline containing 0.1% Tween 20 by incubating overnight at 4°C with gentle shaking (Upadhyay et al 2010). The quality of the BBMVs preparations were accessed with the activity of marker enzymes, alkaline phosphatase (ALP) and leucine aminopeptidase (APN).…”

Section: Insectsmentioning

confidence: 99%

Role of alkaline phosphatase in insecticidal action of Cry1Ac against Helicoverpa armigera larvae

Singh

2011

Biotechnol Lett

Cry1Ac δ-endotoxin produced by Bacillus thuringiensis (Bt) is used as a bio-pesticide for the control of Helicoverpa armigera. Aminopeptidases N (APN) and alkaline phosphatase (ALP) play critical roles in its action against H. armigera larvae. The binding of Cry1Ac with brush border membrane vesicle (BBMV) proteins was increased with the larval development although the sensitivity of larvae to δ-endotoxins decreased. There was higher expression of ALP than APN in early instar larvae with a ~10-fold higher affinity of Cry1Ac towards ALP than to APN. Binding to a specific receptor is therefore more important for the insecticidal activity rather than overall binding to the BBMV proteins. ALP might play a major role in toxicity as compared to APN.