Four patients with recurrent staphylococcal furonculosis and deep abscess formation were evaluated to determine if a defect in the host defense mechanism could account for the unusual incidence of infection. Each also suffered repeated allergic rhinitis, often preceding the onset of infection. A marked defect in neutrophil granulocyte chemotaxis occurred when the patients were symptomatic with rhinitis and abscess formation. Their mean chemotactic index (+/- SD) was 16 +/- 6, while that of 25 control subjects was 70 +/- 11. Neutrophil random migration, phagocytosis, bactericidal activity, and lymphocyte T-cell populations were normal, as were serum concentrations of IgA, IgG, IgM, and IgE. Serial neutrophil function tests revealed normal chemotactic responsiveness when the patients were symptom-free of allergic rhinitis and no longer having abscesses. Abnormal function returned, however, when symptoms recurred. These studies suggest that defective neutrophil function associated with allergic phenomena need not be accompanied by hyperimmunoglobulinemia E. Such defects may be intermittent, appearing when allergic symptomatology and infections develop.

A genetically defined, serologically identified antigen of the rat lymphocyte membrane (AgF-1) has been isolated. Viable spleen and lymph node cells, prepared by Ficoll-Hypaque density centrifugation from Fischer rats, were radioiodinated with soluble lactoperoxidase. Extracts obtained with Nonidet P-40 were shown to contain numerous radiolabeled proteins including cell-surface globulin. AgF-1 was isolated from these extracts by precipitation with a highly specific alloantibody in conjunction with xenospecific anti-globulin antibody and polyethylene glycol (PEG). The use of PEG greatly increased the efficiency of the double antibody technique. The putative antigenic peak was eluted from sodium dodecyl sulfate polyacrylamide gels (SDS-PAGE) and specific antigenic activity was recovered. Removal of the SDS from these eluates was achieved by equilibration with urea and passage over an anion exchange resin. Renaturation, as evidenced by specific inhibition of complement-mediated cytotoxicity, occurred upon the removal of urea by dialysis. The m.w. of the purified antigen was estimated to be 35 to 40,000 daltons by SDS-PAGE and was unaffected by reduction with 2-mercaptoethanol. Amino acid composition was roughly similar to those reported for the major histocompatibility antigens of the rat and other species.