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FIG. 2. Characterization of bacterially expressed and purified H5N1 HA proteins. (A and B) Characterization of purified H5N1 HA proteins from E. coli by Superdex S-200 gel filtration chromatography. Purified H5N1 HA1 proteins with an intact N terminus (positions 1 to 320) (A) and HA1 with an N-terminal deletion (28 to 320) (B) were subjected to gel filtration. The panels show superimposed elution profiles of purified HA1 proteins (red lines) overlaid with calibration standards (gray lines). The elution volumes of protein species are shown in parentheses. (C and D) Steady-state binding equilibrium analysis of conformation-dependent human H5N1 neutralizing MAbs FLD21.40 (C) and FLA3.14 (D) at 10 g/ml to purified bacterially expressed H5N1 HA1 proteins immobilized on a sensor chip through the free amine group and on a blank flow cell, free of peptide. Binding was recorded using a <t>ProteOn</t> system surface plasmon resonance biosensor instrument (Bio-Rad Labs, Hercules, CA). (E) Agglutination of human RBCs by properly folded oligomeric H5N1 rHA1(1-320) protein and its monomeric H5N1 rHA1(28-320) counterpart along with rgH5N1 virus. Serial dilutions of purified HA1 proteins were mixed with washed RBCs, and hemagglutination was read after 30 min at room temperature. Reassorted virus rgH5N1xPR8 (2:6) A/Vietnam/1203/2004 (clade 1) was used as a positive control.
Bio Rad Proteon Manager Software, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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FIG. 2. Characterization of bacterially expressed and purified H5N1 HA proteins. (A and B) Characterization of purified H5N1 HA proteins from E. coli by Superdex S-200 gel filtration chromatography. Purified H5N1 HA1 proteins with an intact N terminus (positions 1 to 320) (A) and HA1 with an N-terminal deletion (28 to 320) (B) were subjected to gel filtration. The panels show superimposed elution profiles of purified HA1 proteins (red lines) overlaid with calibration standards (gray lines). The elution volumes of protein species are shown in parentheses. (C and D) Steady-state binding equilibrium analysis of conformation-dependent human H5N1 neutralizing MAbs FLD21.40 (C) and FLA3.14 (D) at 10 g/ml to purified bacterially expressed H5N1 HA1 proteins immobilized on a sensor chip through the free amine group and on a blank flow cell, free of peptide. Binding was recorded using a ProteOn system surface plasmon resonance biosensor instrument (Bio-Rad Labs, Hercules, CA). (E) Agglutination of human RBCs by properly folded oligomeric H5N1 rHA1(1-320) protein and its monomeric H5N1 rHA1(28-320) counterpart along with rgH5N1 virus. Serial dilutions of purified HA1 proteins were mixed with washed RBCs, and hemagglutination was read after 30 min at room temperature. Reassorted virus rgH5N1xPR8 (2:6) A/Vietnam/1203/2004 (clade 1) was used as a positive control.

Journal: Journal of Virology

Article Title: H5N1 Virus-Like Particle Vaccine Elicits Cross-Reactive Neutralizing Antibodies That Preferentially Bind to the Oligomeric Form of Influenza Virus Hemagglutinin in Humans

doi: 10.1128/jvi.05406-11

Figure Lengend Snippet: FIG. 2. Characterization of bacterially expressed and purified H5N1 HA proteins. (A and B) Characterization of purified H5N1 HA proteins from E. coli by Superdex S-200 gel filtration chromatography. Purified H5N1 HA1 proteins with an intact N terminus (positions 1 to 320) (A) and HA1 with an N-terminal deletion (28 to 320) (B) were subjected to gel filtration. The panels show superimposed elution profiles of purified HA1 proteins (red lines) overlaid with calibration standards (gray lines). The elution volumes of protein species are shown in parentheses. (C and D) Steady-state binding equilibrium analysis of conformation-dependent human H5N1 neutralizing MAbs FLD21.40 (C) and FLA3.14 (D) at 10 g/ml to purified bacterially expressed H5N1 HA1 proteins immobilized on a sensor chip through the free amine group and on a blank flow cell, free of peptide. Binding was recorded using a ProteOn system surface plasmon resonance biosensor instrument (Bio-Rad Labs, Hercules, CA). (E) Agglutination of human RBCs by properly folded oligomeric H5N1 rHA1(1-320) protein and its monomeric H5N1 rHA1(28-320) counterpart along with rgH5N1 virus. Serial dilutions of purified HA1 proteins were mixed with washed RBCs, and hemagglutination was read after 30 min at room temperature. Reassorted virus rgH5N1xPR8 (2:6) A/Vietnam/1203/2004 (clade 1) was used as a positive control.

Article Snippet: Binding kinetics for the selected human vaccine sera and data analyses were calculated using Bio-Rad ProteOn manager software (version 2.0.1).

Techniques: Chromatography, Binding Assay, SPR Assay, Agglutination, Virus, Positive Control