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. 2000 Sep;12(9):1783–1794. doi: 10.1105/tpc.12.9.1783

Table 1.

Alkalinization-Inducing Activity and Binding Activity of Flagellin and Flagellin-Derived Peptides

Protein or Peptide Amino Acid Sequencea Biological Activity
EC50 (nM)b
Binding Affinity
IC50 (nM)c
Flagellin Intact protein, 33 kD 0.30 120
Tyr-flg22 YQRLSTGSRINSAKDDAAGLQIA 0.03 1
flg22 QRLSTGSRINSAKDDAAGLQIA 0.03 2
flg15 RINSAKDDAAGLQIA 0.06 7
flg15-Δ3 RINSAKDDAAGL 15.00 80
flg15-Δ4 RINSAKDDAAG Antagonist 400
flg15-Δ7 RINSAKDD Antagonist 400
flg13 NSAKDDAAGLQIA 75.00 600,000
flg8 DAAGLQIA Inactive Inactive
flg15-swap8-9 RINSAKDADAGLQIA 14.00 12,000
flg15A.tum. RVGDASDNAAYWSIA Inactive Inactive
flg15R.mel. RVGQAADNAAYWSIA Inactive Inactive
flg15E.coli RINSAKDDAAGQAIA 0.20 6
Systemin AVQSKPPSKRDPPKMQTD Inactive Inactive
a

Amino acid sequence of synthetic peptides used. Amino acids underlined indicate differences from the sequence in Pseudomonas aeruginosa.

b

Concentration that induces half-maximal alkalinization response in tomato cells. Some of the values are reproduced from Felix et al. (1999). Inactive, no significant alkalinization response when tested in concentrations up to 10 μM (EC50 >> 10,000 nM).

c

Concentration required to reduce binding of 125I-Tyr-flg22 to microsomal membranes by 50% when measured after 20 min of incubation at 4°C. Inactive, no significant competition when tested in concentrations up to 100 μM (IC50 >> 100,000 nM).