Recombinant Mouse Antibody (19D9D6) is capable of binding to F. magna PpL (D55A), expressed in Chinese Hamster Ovary cells (CHO). mAb 19D9D6 appeared to be specific for an epitope encompassed by residues 29–33 within the main antigenic domain, a property shared by the major human epitope of core.
Figure 1 HCV core peptide 13–40 bound by Fab 19D9D6 and comparison with its solution conformation.
a, Ball-and-stick representation showing the Fab-bound peptide (magenta, glycines in green) conformation (hydrogen bonds in yellow). b, Residues 29–39 of HCV core extracted from the solution NMR structure (PDB-ID: 1CWX:3) (14, 15) so that the epitope residues IVGGVYLL are approximately oriented as in a. V31 and I30 do not superpose well. c, Stereoscopic representation of the electron density in the final Fo-Fc A omit-refine map around the Ag binding site showing the bound peptide. d, Stereoscopic representation of the superposition of the solution structure (14, 15) on the Fab 19D9D6-bound core peptide residues 25–40 (x-ray model). A good overlap can be achieved over the GGVYL stretch. To bind, Fab 19D9D6 must induce a rearrangement about G32-G33. e, Light chain (light blue) interaction made with the HCV peptide. The heavy chain is shown as a surface. f, Heavy chain residues (dark blue) that interact with the peptide. The light chain is shown in surface representation.
Ménez, R., Bossus, M., Muller, B. H., Sibaï, G., Dalbon, P., Ducancel, F., ... & Stura, E. A. (2003). Crystal structure of a hydrophobic immunodominant antigenic site on hepatitis C virus core protein complexed to monoclonal antibody 19D9D6. The Journal of immunology, 170(4), 1917-1924.
Figure 2 Competition ELISA between peptides.
The inhibition curve for 13–40 (continuous line) shows that the shorter peptide out-competes the longer one (2–45; broken line) by a factor of 10–50. The two peptides have a similar behavior at low peptide concentrations, but at higher peptide concentrations, 2–45 is a less effective competitor than 13–40, possibly due to some degree of aggregation (to be verified by other techniques) of the 2–45 peptide.
Ménez, R., Bossus, M., Muller, B. H., Sibaï, G., Dalbon, P., Ducancel, F., ... & Stura, E. A. (2003). Crystal structure of a hydrophobic immunodominant antigenic site on hepatitis C virus core protein complexed to monoclonal antibody 19D9D6. The Journal of immunology, 170(4), 1917-1924.
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CAT | Product Name | Application | Type |
---|---|---|---|
MOB-795 | Recombinant Anti-Peptostreptococcus. spp PpL Antibody | ELISA, IP, FuncS | IgG |
MHH-795 | Recombinant Human Anti-Peptostreptococcus. spp PpL Antibody | IF, Neut, FuncS | IgG |
PABZ-042 | Recombinant Human Anti-F. magna PpL Antibody (2A2) | ELISA | IgG |
CAT | Product Name | Application | Type |
---|---|---|---|
MOB-795-F(E) | Recombinant Anti-Peptostreptococcus. spp PpL Antibody Fab Fragment | WB, ELISA, FuncS | Fab |
MHH-795-F(E) | Recombinant Human Anti-Peptostreptococcus. spp PpL Antibody Fab Fragment | IF, FC, FuncS | Fab |
PFBZ-042 | Recombinant Human Anti-F. magna PpL Antibody Fab Fragment (2A2) | ELISA | |
PFBW-042 | Recombinant Mouse Anti-F. magna PpL (D55A) Antibody Fab Fragment (19D9D6) | ELISA, BL | IgG |
CAT | Product Name | Application | Type |
---|---|---|---|
MOB-795-S(P) | Recombinant Anti-Peptostreptococcus. spp PpL Antibody scFv Fragment | IP, IF, Biosensors, FuncS | scFv |
MHH-795-S(P) | Recombinant Human Anti-Peptostreptococcus. spp PpL Antibody scFv Fragment | ELISA, WB, IF, FuncS | scFv |
PSBZ-042 | Recombinant Human Anti-F. magna PpL Antibody scFv Fragment (2A2) | ELISA | scFv |
PSBW-042 | Recombinant Mouse Anti-F. magna PpL (D55A) Antibody scFv Fragment (19D9D6) | ELISA, BL | scFv |
CAT | Product Name | Application | Type |
---|---|---|---|
MOR-2810 | Hi-Affi™ Recombinant Rabbit Anti-PPL Monoclonal Antibody (DS2810AB) | WB, IHC | IgG |
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