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Fig. 1 . Investigated downstream procedure. Suitability of
anion-exchange (Q-Sepharose XL) followed by size exclusion Superdex 200
prep grade (pg) for capturing and polishing step. Q-Sepharose XL was fed
with 20 fold concentrate of primary feed stock obtained from tangential
flow filtration. A final concentration step was included after polishing
step for decrease purified sample volume. Then Tris-HCl buffer was
replaced by phosphate buffer through diafiltration (DF) before
inactivation and formulation.
Fig. 2 . Elution profile of FMDV from 400×16 mm, I.D. column of
Q-sepharose XL (A). Crude FMDV was loaded after dilution with initial
buffer, Tris-HCl (20 mM, pH 7.3) and then eluted with elution buffer,
Tris-HCl (20 mM, pH 7.3 containing 500 mM KCl). Separation conditions
were set as follows: volume of injection: 50 mL, dilution factor: 6,
flow rate for sample loading: 3 mL/min, flow rate for elution step: 8
mL/min. Pooled virus fraction was collected from first dimension and
applied to the 600×26 mm, I.D. column of Sup-200 stationary phase in the
second dimension (B). Separation conditions were set as follows: mobile
phase composed 20 mM Tris-HCl (150 mM NaCl, pH 7.3), flow rate 2.5
mL/min and injection volume 4 mL. Chromatograms in both dimension were
recorded at 280 nm.
Fig. 3 . Elution profile of FMDV from 400×16 mm, I.D. column of
Q-Sepharose XL (A). Crude FMDV was loaded after dilution with initial
buffer, Tris-HCl (20 mM, pH 7.3) and then eluted with elution buffer,
Tris-HCl (20 mM, pH 7.3 containing 500 mM KCl). Separation conditions
were set as follows: volume of injection: 100 mL, dilution factor: 6,
flow rate for sample loading: 3 mL/min, flow rate for elution step: 8
mL/min. Pooled virus fraction was collected from first dimension and
applied to the 600×26 mm, I.D. column of Sup-200 stationary phase in the
second dimension (B). Separation conditions were set as follows: mobile
phase composed 20 mM Tris-HCl (150 mM NaCl, pH 7.3), flow rate 2.5
mL/min and injection volume 4 mL. Chromatograms in both dimension were
recorded in 280 nm.
Fig. 4. Application HP-SEC on Ultrahydrogel Linear (300 × 7.8
mm, I.D.) analytical column for evaluation fingerprint elution profile
during three stage purification strategy. Solid line (Primary crude
sample), Dash line (Intermediate concentration step), Dotted line
(Second dimension). HP-SEC was performed as follows: mobile phase; 0.1 M
Na2SO4 in 50 mM PBS (pH7.0), injection volume: 50 µl, flow-rate, 0.6
mL/min and detection wavelength: 280 nm.
Fig. 5. SDS–PAGE of purified FMDV vaccine. Lane 1, Protein
markers; Lane 2, 2D-AEC×SEC purified FMDV. The identity of the final
product from 2D-AEC×SEC was confirmed by presence of VP1-3 in 20-35 kD
and VP4 in10 kD.
Fig 6. MALDI-TOF-MS profiles of purified FMDV particles by
2D-AEC×SEC in low molecular weight 2–20 kD (A ),medium molecular weight 20–50 kD (B ) and high molecular weight
50-100 kD (C ).
Fig 7. Characterization of purified FMDV particles by (A) DLS
analysis and (B) TEM imaging.