Overexpression (OE-FLA11) and mutation analyses demonstrate FLA11’s role in:
SCW Thickening: OE-FLA11 plants exhibit 20–30% thicker SCWs compared to wild-type (WT) .
Lignin-Cellulose Dynamics: Increased lignin content (15–20% higher) with reduced crystalline cellulose (10–15% lower) .
Mechanical Stress Sensing: FLA11 upregulates stress-response genes (e.g., NST1, NST3) under tensile or compressive forces .
| Mutation | Fiber Length Reduction | SCW Thickness Increase | Lignin S:G Ratio |
|---|---|---|---|
| AG1 modification | 25%* | 30%* | 1.2 → 0.8* |
| GPI anchor removal | 15% | 10% | No change |
| N-glycosylation | 20% | 25% | 1.2 → 0.9 |
| *Data normalized to WT; *p < 0.01. |
FLA11 antibodies are critical for:
Immunogold Localization: Anti-His/YFP antibodies (e.g., 1:100 dilution) label FLA11 at SCWs using transmission electron microscopy .
Protein Blot Analysis: Detects ~60 kDa core protein and ~110 kDa glycosylated forms .
Mutant Validation: Confirms disrupted AG glycosylation or GPI anchoring in transgenic lines .
Antibody specificity for FLA11 is confirmed through:
Knockout Controls: fla11/fla12 double mutants show no signal .
Orthogonal Methods: Cross-validation with RNA-seq and lignin quantification .
Independent Antibodies: Anti-AGP antibodies corroborate FLA11 localization .
| Method | Application in FLA11 Studies | Outcome |
|---|---|---|
| Genetic (KO lines) | Confirm absence in fla11 mutants | No false positives |
| Immunocapture-MS | Identify bound SCW proteins | FLA11 interacts with cellulose synthases |
| Recombinant tagging | HIS/YFP fusion proteins | 100% specificity for FLA11 |
Redundancy: Functional overlap with FLA12 complicates phenotype isolation .
Glycan Shield Complexity: AG glycosylation variability affects antibody-epitope accessibility .
Therapeutic Potential: No direct medical applications reported yet, but insights may inform bioengineering of plant-based materials .