The osmotic virial coefficient B2 of globular protein solutions is calculated as a function of added salt concentration at fixed pH by computer simulations of the "primitive model." The salt and counterions as well as a discrete charge pattern on the protein surface are explicitly incorporated. For parameters roughly corresponding to lysozyme, we find that B2 first decreases with added salt concentration up to a threshold concentration, then increases to a maximum, and then decreases again upon further raising the ionic strength. Our studies demonstrate that the existence of a discrete charge pattern on the protein surface profoundly influences the effective interactions and that linear and nonlinear Poisson Boltzmann theories fail for large ionic strength. The observed nonmonotonicity of B2 is compared with experiments. Implications for protein crystallization are discussed.