Supplemental Data
Files in this Data Supplement:
- Supplementary S2 (.jpg, 1.6 MB) - Supplementary S2. (A) No iron-binding activity was detected for recombinant Pv. The x-axis indicates the protein concentration and the y-axis indicates the OD ratio at 630 nm. (B and C) No difference was found in the antimicrobial activity of recombinant Pv against E. coli (B) and S. aureus (C) in the presence or absence of excess iron. The x-axis indicates time and the y-axis indicates the OD at 630 nm. Each point in the graphs represents the mean values of at least three experiments.
- Supplementary S4 (.jpg, 158 KB) - Supplementary S4. SDS-PAGE of truncated phosvitins with N-terminus or C-terminus deleted. They were expressed in E. coli and purified. lane M, standard molecular mass; Pt1 (55-249), Pt2 (102-249), Pt3 (134-249), Pt4 (174-249), Pt5 (194-249) and Pt6 (1-194) represented different truncated peptides.
- Supplementary S1 (.jpg, 745 KB) - Supplementary S1. Identification of recombinant Pv. A. SDS-PAGE. lane 1, standard molecular mass; lane 2, total cellular extracts from E. coli BL21 containing pET28a/Pv before induction; lane 3, total cellular extracts from IPTG-induced E. coli BL21 containing pET28a/Pv; lane 4, recombinant Pv purified on Ni-NTA resin column. B. MALDI/TOF MS mapping of the purified protein.
- Supplementary S5 (.jpg, 588 KB) - Supplementary S5. Saturation curve of the binding of m12 and m13 to various ligands. (A) Binding of m12 to LPS, LTA and PGN. (B) Binding of m13 to LPS, LTA and PGN. The affinities of m12 and m13 to LPS, LTA and PGN were significantly reduced compared to those of Pt5.
- Supplementary S3 (.jpg, 202 KB) - Supplementary S3. SDS-PAGE. lane M, standard molecular mass; lane 1, rPv; lane 2, FITC-labeled rPv. FITC-labeled rPv appeared as a single band on a SDS-PAGE, suggesting that FITC-labeled rPv remained as monomer.
