Deadly Fungal Effector: His-GST-TRP Induces Rapid Cell Death in Arabidopsis Protoplasts

Original video: https://youtu.be/zc77L02q8K4 A fungal effector that is toxic to plant cells was identified in Verticillium dahliae. The effector contains a non-canonical Common in several Fungal Extracellular Membrane proteins (CFEM) domain, a tandem repeat region consisting of four 14-amino acid repeats rich in proline, and a C-terminal region, thus is designated V. dahliae tetrapeptide repeat protein (VdTRP). The membrane targeting of VdTRP is vital for its cell toxicity. CFEM mediates the membrane targeting and the tandem repeat region exerts the toxic function upon cell membrane. The chitinase-like 1 (CTL1), an essential apoplastic protein of cotton, can redirect VdTRP from cell membrane to apoplast.

This video showcases the dramatic difference in toxicity between the fungal effector protein His-GST-TRP and its control, His-GST, when expressed in Arabidopsis protoplasts. Watch as the expression of His-GST-TRP triggers rapid cell death, highlighting its potent toxic effect on plant cells. His-GST-TRP is a protein construct that was expressed in E. coli and purified. It represents the full-length VdTRP protein with an N-terminal His-GST tag. This construct was used in lipid binding assays and in experiments to assess its toxicity in comparison to other modified versions of VdTRP. While His-GST is an empty vector control, suggesting that the His-GST tag alone was expressed and used as a baseline in the experiments

Keywords: His-GST-TRP, His-GST, Arabidopsis protoplasts, cell death, fungal effector, toxicity, plant cells, control protein, visual comparison, microscopy, time-lapse, live imaging, TRP domain, VdTRP, Verticillium dahliae, plant pathology, effector protein, protein toxicity, cell biology, molecular biology.

Citation:

Liu, H., Zhang, W., He, Q. et al. Re-localization of a repeat-containing fungal effector by apoplastic protein Chitinase-like 1 blocks its toxicity. Nat Commun 15, 10122 (2024). https://doi.org/10.1038/s41467-024-54470-0

Published on: 22 November 2024

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