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1H, 13C and 15N NMR assignments of two plant protease inhibitors (IRD7 and IRD12) from the plant Capsicum annuum

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Abstract

Helicoverpa species are polyphagous pests, with the larval stages causing major damage to economically valuable crops such as cotton, tomato, corn, sorghum, peas, sunflower, wheat and other pulses. Over the years, Helicoverpa armigera has developed resistance to most classes of chemical insecticides, and consequently it is now largely controlled on cotton plants via the use of Bt transgenic crops that express insecticidal Cry toxins which in-turn expedited resistance development in a number of pest species including H. armigera. In a hope to provide other eco-friendly alternatives solutions to counter the effect of the pest, people have identified a number of protease inhibitors (PIs) from the domesticated capsicum species Capsicum annuum, several of which potently inhibited H. armigera gut proteases and impeded growth of H. armigera larva. With a view to explore and enhance the specific nature or properties of these PIs on the mechanism of inhibition, structural and functional characterization of these PIs are inevitable. Towards this goal, we have carried out complete 1H, 13C and 15N resonance assignments of two of these PIs, identified as IRD7 and IRD12, using a suite of 2D and 3D multi-dimensional and multi-nuclear NMR experiments.

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Abbreviations

IRD:

Inhibitory repeating domains

HSQC:

Heteronuclear single quantum correlation

NMR:

Nuclear magnetic resonance

PI:

Protease inhibitors

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Acknowledgements

We acknowledge financial support from the Indian Department of Science and Technology (Indo-Australian joint project DST/INT/AUS/P-63/2015 to K.V.R.C.), UGC-faculty recharge program and DST-ECR/2017/000124 to R.P.B., Australia-India Strategic Research Fund (AISRF-1277949-197), Department of Biotechnology (DBT), Council of Scientific and Industrial Research (CSIR), Tata Institute of Fundamental Research (TIFR), and the Australian National Health & Medical Research Council (Principal Research Fellowship APP1136889 to G.F.K.). We also acknowledge the Indian National Facility of High Field NMR.

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Authors and Affiliations

  1. Center for Interdisciplinary Sciences, Tata Institute of Fundamental Research, Gopanpally, Hyderabad, 500075, India

    Janeka Gartia & Kandala V. R. Chary

  2. Department of Biophysics, Panjab University, Chandigarh, 160014, India

    Ravi Pratap Barnwal

  3. Institute for Molecular Bioscience, University of Queensland, Brisbane, QLD, 4072, Australia

    Raveendra Anangi & Glenn King

  4. CSIR-National Chemical Laboratory, Pune, 411008, India

    Ashok R. Giri

  5. Department of Chemical Sciences, Tata Institute of Fundamental Research, 1, Homi Bhabha RoadColaba, Mumbai, 400005, India

    Kandala V. R. Chary

  6. Indian Institute of Science Education and Research, Berhampur, Odisha, 760010, India

    Kandala V. R. Chary

Authors
  1. Janeka Gartia
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  2. Ravi Pratap Barnwal
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  3. Raveendra Anangi
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  4. Ashok R. Giri
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  5. Glenn King
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  6. Kandala V. R. Chary
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Correspondence to Kandala V. R. Chary.

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Gartia, J., Barnwal, R.P., Anangi, R. et al. 1H, 13C and 15N NMR assignments of two plant protease inhibitors (IRD7 and IRD12) from the plant Capsicum annuum. Biomol NMR Assign 13, 31–35 (2019). https://doi.org/10.1007/s12104-018-9846-z

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