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C-terminus processing in Tma12 is critical for its insecticidal activity.

Bhawana Gupta1, Pooja Singh1, Pradhyumna Kumar Singh1

  • 1Molecular Biology and Biotechnology Division, CSIR-National Botanical Research Institute, Rana Pratap Marg, Lucknow 226001, Uttar Pradesh, India; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad 201002, Uttar Pradesh, India.

International Journal of Biological Macromolecules
|November 6, 2024
PubMed
Summary
This summary is machine-generated.

Tma12, a fern-derived biopesticide, requires a specific C-terminus for its insecticidal activity against whiteflies. Protein stability is also enhanced by N-linked glycosylation, crucial for its efficacy.

Keywords:
BiopesticideGlycosylationKM71HLPMOPichia pastorisTma12Whitefly

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Area of Science:

  • Biochemistry
  • Entomology
  • Plant Science

Background:

  • Tma12 is a fern-derived biopesticide with known LPMO activity linked to insecticidal properties.
  • Previous structural analysis indicated potential C-terminus processing of Tma12.

Purpose of the Study:

  • To investigate the role of the Tma12 protein C-terminus in its insecticidal activity.
  • To determine the impact of N-linked glycosylation on Tma12 protein stability and function.

Main Methods:

  • Expression of (His)6-tagged Tma12 in Pichia.
  • Analysis of different Tma12 protein forms (30 kDa and 24 kDa).
  • Deletion mutagenesis to confirm C-terminus processing and assessment of glycosylation-defective mutants.

Main Results:

  • A 24 kDa Tma12 protein form showed significant toxicity to whiteflies (LC50 1.38 μg/ml), while a 30 kDa form did not.
  • Absence of the (His)6 tag in the active 24 kDa form indicated C-terminus processing, confirmed by mutagenesis.
  • Glycosylation-defective Tma12 mutants failed to express, highlighting the importance of glycans for protein stability.

Conclusions:

  • The C-terminus of Tma12 is critical for its anti-whitefly activity, in addition to its N-terminal catalytic center.
  • N-linked glycosylation plays a vital role in maintaining the stability of the Tma12 protein.