Protease and Inhibitor Data for Pythium Antagonist-Host Interactions

Transcriptome and exo-proteomic analysis identified 25 proteases with significantly higher abundance in the microbial antagonist Pythium oligandrum when cultured with host material. Two Kazal-type serine protease inhibitors from the host Pythium myriotylum were heterologously produced, with one (Pm_KSPI-11) showing strong inhibitory activity against trypsin. The dataset, authored by Jinhao Chen and last updated in May 2026, supports research into biological control mechanisms for crop diseases.

Use Cases

• Training models to predict protease-inhibitor interactions based on protein sequence and modeling data.
• Analyzing gene expression patterns related to protease activity in microbial antagonists.
• Studying the efficacy of specific protease inhibitors (e.g., Pm_KSPI-11) in reducing pathogen growth in vitro.

Strengths

• Includes quantitative inhibition constant (Ki) data for a key protease inhibitor (Pm_KSPI-11).
• Analysis is based on transcriptomic and exo-proteomic methods, suggesting a multi-omics foundation.
• Dataset is openly available under a CC-BY-4.0 license.

Limitations

• Column-level documentation is absent; field semantics must be inferred after download.
• Row count is unknown, which may limit suitability assessment for large-scale ML tasks.
• The 18.5 MB size indicates a relatively small dataset, potentially limiting statistical power.

Provenance

Source

figshare

Collection Method

Likely contains experimental data from transcriptome analysis, exo-proteomic profiling, and heterologous protein production assays.

Freshness

Last updated 2026-05-17 03:58:21; freshness should be verified.