Successive absorption of pooled normal human serum by six strains of Salmonella typhimurium having different lipopolysaccharide composition removed strain-specific antibody and cross-reactive antibody. Cross-reactive antibody, as demonstrated by quantitative fluorescence, made some contribution to the ingestion of smooth strain (SH 2201) while anti-smooth antibody was not necessary for the opsonization of rough mutants. It was also demonstrated that anti-SR antibody (IgG) was effective in the opsonization of SR and S strains. The deposition of antibody on the surface of Ra strain was not reduced by absorption of serum by any organisms other than Ra. On the other hand, cross-reactive antibody had a small effect on the ingestion of Ra; this may be due to antibody other than IgG. Those strains ingested by neurtophils predominantly though complement activation in the presence of antibody were s, SR, and Rb2. The effect of cross-reactive antibody was none for Rb2 strain, slight for SR strain and some for s strain. It suggests that cross reactive antibody can afford immune protection though the enhancement of opsonization, especially noticeable on the ingestion of smooth strain by neurtrophils.