Provided are antibodies bind to the NIm-IA site of HRV14, which is the β-B–β-C loop of the viral capsid protein VP1. Two antibodies, Fab17-IA (Fab17) and Fab12-IA (Fab12), bind bivalently to the virion surface and strongly neutralize viral infectivity whereas Fab1-IA (Fab1) strongly aggregates and weakly neutralizes virions. All of the antibodies contact a significant proportion of the canyon region and directly overlap much of the receptor (intercellular adhesion molecule 1 [ICAM-1]) binding site. Fab1, however, does not contact the same residues on the upper south wall (the side facing away from fivefold axes) at the receptor binding region as do Fab12 and Fab17. All three antibodies cause some stabilization of HRV14 against pH-induced inactivation; thus, stabilization may be mediated by invariant contacts with the canyon.
Figure 1 Neutralization (○) and precipitation (△) properties of the NIm-IA antibodies MAb1 (strong precipitator, weak neutralizer).
MAb1-IA only weakly inhibited plaque formation, with a maximum inhibition of ~2 orders of magnitude and with a slight enhancement in neutralization at intermediate antibody/virus ratios. MAb1-IA strongly aggregated the virions over the same range of ratios at which neutralization enhancement was observed. At very high antibody/virus ratios, there was little precipitation but significant (~1.5-log-unit) neutralization. Therefore, MAb1-IA does not neutralize HRV14 solely by precipitating it, but neutralization is enhanced by aggregation at intermediate antibody/virus ratios.
Che, Z., Olson, N. H., Leippe, D., Lee, W. M., Mosser, A. G., Rueckert, R. R., ... & Smith, T. J. (1998). Antibody-mediated neutralization of human rhinovirus 14 explored by means of cryoelectron microscopy and X-ray crystallography of virus-Fab complexes. Journal of virology, 72(6), 4610-4622.
Figure 2 Saturation (A) and aggregation (B) curves for MAb17-1A(■) and MAbl-IA (□).
A weakly neutralizing aggregating antibody that binds to the same site (MlAbl-IA) binds with a stoichiometry of approximately 60 MlAbl-IA molecules per virion.
Smith, T. J., Olson, N. H., Cheng, R. H., Liu, H. A. N. S. O. N. G., Chase, E. S., Lee, W. M., ... & Baker, T. S. (1993). Structure of human rhinovirus complexed with Fab fragments from a neutralizing antibody. Journal of virology, 67(3), 1148-1158.
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CAT | Product Name | Application | Type |
---|---|---|---|
HPAB-M0531-YC | Recombinant Mouse Anti-HRV14 NIm-IA Antibody (MAb17-IA) | ELISA, Neut (strong), Precipitation (weak) | Mouse IgG |
HPAB-M0532-YC | Recombinant Mouse Anti-HRV14 NIm-IA Antibody (MAb12-IA) | Neut (strong), Precipitation (weak) | Mouse IgG2a |
CAT | Product Name | Application | Type |
---|---|---|---|
HPAB-M0531-YC-S(P) | Recombinant Mouse Anti-HRV14 NIm-IA Antibody scFv Fragment (MAb17-IA) | ELISA, Neut (strong), Precipitation (weak) | Mouse scFv |
HPAB-M0532-YC-S(P) | Recombinant Mouse Anti-HRV14 NIm-IA Antibody scFv Fragment (MAb12-IA) | Neut (strong), Precipitation (weak) | Mouse scFv |
HPAB-M0533-YC-S(P) | Recombinant Mouse Anti-HRV14 NIm-IA Antibody scFv Fragment (MAb1-IA) | Neut (weak), Precipitation (strong) | Mouse scFv |
CAT | Product Name | Application | Type |
---|---|---|---|
HPAB-M0531-YC-F(E) | Recombinant Mouse Anti-HRV14 NIm-IA Antibody Fab Fragment (MAb17-IA) | ELISA, Neut (strong), Precipitation (weak) | Mouse Fab |
HPAB-M0532-YC-F(E) | Recombinant Mouse Anti-HRV14 NIm-IA Antibody Fab Fragment (MAb12-IA) | Neut (strong), Precipitation (weak) | Mouse Fab |
HPAB-M0533-YC-F(E) | Recombinant Mouse Anti-HRV14 NIm-IA Antibody Fab Fragment (MAb1-IA) | Neut (weak), Precipitation (strong) | Mouse Fab |
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