Changes and induction of aminopeptidase activities in response to pathogen infection during germination of pigeonpea (Cajanas cajan) seeds

Lomate, Purushottam R.; Hivrale, Vandana K.

doi:10.1016/j.jplph.2011.05.002

Cited by 8 publications

(4 citation statements)

References 52 publications

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“…Thus, during this current scenario of host-pest co-evolution, pigeonpea (Cajanus cajan), a crop plant of the order Fabales, family Leguminosae has been reported as the potential source of (PIs) against wide varieties of lepidopteran larvae (Chougule et al, 2003;Lomate and Hivrale, 2011;Padul et al, 2012;Parde et al, 2012;Prasad et al, 2010aPrasad et al, , 2010bPrasad et al, , 2009. Earlier reports suggested that different varieties of C. cajan possessed PIs resistant to proteases of A. janata (Prasad et al, 2010a(Prasad et al, , 2009.…”

Section: Introductionmentioning

confidence: 99%

Structural and functional characterization of proteinase inhibitors from seeds of Cajanus cajan (cv. ICP 7118)

Swathi

Lokya

Swaroop

et al. 2014

Plant Physiology and Biochemistry

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Proteinase inhibitors (C11PI) from mature dry seeds of Cajanus cajan (cv. ICP 7118) were purified by chromatography which resulted in 87-fold purification and 7.9% yield. SDS-PAGE, matrix assisted laser desorption ionization time-of-flight (MALDI-TOF/TOF) mass spectrum and two-dimensional (2-D) gel electrophoresis together resolved that C11PI possessed molecular mass of 8385.682 Da and existed as isoinhibitors. However, several of these isoinhibitors exhibited self association tendency to form small oligomers. All the isoinhibitors resolved in Native-PAGE and 2-D gel electrophoresis showed inhibitory activity against bovine pancreatic trypsin and chymotrypsin as well as Achaea janata midgut trypsin-like proteases (AjPs), a devastating pest of castor plant. Partial sequences of isoinhibitor (pI 6.0) obtained from MALDI-TOF/TOF analysis and N-terminal sequencing showed 100% homology to Bowman-Birk Inhibitors (BBIs) of leguminous plants. C11PI showed non-competitive inhibition against trypsin and chymotrypsin. A marginal loss (<15%) in C11PI activity against trypsin at 80 (°)C and basic pH (12.0) was associated with concurrent changes in its far-UV CD spectra. Further, in vitro assays demonstrated that C11PI possessed significant inhibitory potential (IC50 of 78 ng) against AjPs. On the other hand, in vivo leaf coating assays demonstrated that C11PI caused significant mortality rate with concomitant reduction in body weight of both larvae and pupae, prolonged the duration of transition from larva to pupa along with formation of abnormal larval-pupal and pupal-adult intermediates. Being smaller peptides, it is possible to express C11PI in castor to protect them against its devastating pest A. janata.

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Section: Introductionmentioning

confidence: 99%

Structural and functional characterization of proteinase inhibitors from seeds of Cajanus cajan (cv. ICP 7118)

Swathi

Lokya

Swaroop

et al. 2014

Plant Physiology and Biochemistry

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“…To determine the enzymatic activity of rTsAP, the serially diluted rTsAP (0, 0.004, 0.008, 0.016, 0.032, 0.064 and 0.128 μg/μL) was pre-incubated at 37 °C for 10 min in various pH buffers (pH 4.0-5.0 sodium acetate, pH 6.0-7.0 sodium phosphate, pH 8.0-9.0 Tris-HCl, and pH 10.0-11 sodium bicarbonate) [44]. Subsequently, the aminopeptidase substrate 1 mM Leu-P-nitroaniline (Leu-pNA, Sigma-Aldrich, USA) was added into the reaction mixture and incubated at different temperatures (20-100 °C) for 15 min [45], and the absorbance at 405 nm was measured with a spectrophotometer.…”

Section: Enzymatic Activity Assay Of Rtsapmentioning

confidence: 99%

Characterization of a Trichinella spiralis aminopeptidase and its participation in invasion, development and fecundity

Guo

Bai

Ren

et al. 2020

Vet Res

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A Trichinella spiralis aminopeptidase (TsAP) has been identified in intestinal infectious larvae (IIL) and adult worms (AW), but its biological function in the T. spiralis life cycle is unknown. The aim of this study was to characterize TsAP and ascertain its functions in the invasion, development and fecundity of T. spiralis. Recombinant TsAP (rTsAP) was expressed and purified. rTsAP has strong immunogenicity. qPCR and western blotting show that TsAP was transcribed and expressed at all T. spiralis lifecycle stages, but the expression level of TsAP mRNA and proteins at IIL and AW stages was obviously higher than those in muscle larvae (ML) and newborn larvae (NBL). The IFT results reveal that TsAP was principally located at the cuticle and the intrauterine embryos of this nematode. rTsAP had the enzymatic activity of natural aminopeptidase to hydrolyze the substrate Leu-pNA with an optimal temperature of 50 °C and optimal pH of 8.0. rTsAP promoted the larval penetration into intestinal epithelial cells, whereas anti-rTsAP antibodies suppressed the larval intrusion; the promotion and suppression was dose-dependently related to rTsAP or anti-rTsAP antibodies. TsAP protein expression level and enzymatic activity were reduced by 50.90 and 49.72% through silencing of the TsAP gene by specific siRNA 842. Intestinal AW and muscle larval burdens, worm length and female reproductive capacity were significantly declined in mice infected with siRNA-transfected ML compared to the control siRNA and PBS group. These results indicate that TsAP participates in the invasion, development and fecundity of T. spiralis and it might be a candidate target for anti-Trichinella vaccines.

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“…niger. These findings could be helpful to further dissect a defensive role of aminopeptidases in seed germination which is an important event in plant's life [11].…”

Section: Introductionmentioning

confidence: 97%

The effect of yellow–brown and black soil on the germination of the peanut

BaoPing

2016

Acta Ecologica Sinica

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Changes and induction of aminopeptidase activities in response to pathogen infection during germination of pigeonpea (Cajanas cajan) seeds

Cited by 8 publications

References 52 publications

Structural and functional characterization of proteinase inhibitors from seeds of Cajanus cajan (cv. ICP 7118)

Structural and functional characterization of proteinase inhibitors from seeds of Cajanus cajan (cv. ICP 7118)

Characterization of a Trichinella spiralis aminopeptidase and its participation in invasion, development and fecundity

The effect of yellow–brown and black soil on the germination of the peanut

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