Crystallization and preliminary X-ray diffraction studies of a monoclonal antibody Fab fragment against foot-and-mouth disease virus and of its complex with the main antigenic site peptide.

Abstract

The Fab fragment of the neutralizing monoclonal antibody SD6 elicited against foot-and-mouth disease virus (FMDV) C-S8c1 and its complex with a peptide, corresponding to the major antigenic site of FMDV (VP1 residues 136-150, YTASARGDLAHLTTT), have been crystallized using the hanging drop vapor diffusion techniques. For the isolated Fab, crystals diffracting to 2.5 A resolution were obtained at room temperature using ammonium sulfate as precipitant. These crystals are monoclinic, space group C2, and unit cell parameters a = 109.53 A, b = 89.12 A, c = 64.04 A, and beta = 112.9 degrees and contain one Fab molecule per asymmetric unit. Crystals from the complex diffract, at least, to 2.8 A resolution and were obtained, at room temperature, using PEG as precipitant. These crystals are monoclinic, space group P2, and unit cell parameters a = 56.11 A, b = 60.67 A, c = 143.45 A, and beta = 95.4 degrees. Density packing considerations indicate that there are two Fab molecules in the asymmetric unit.