. The ability of antibodies to cell-surface components of to increase surface hydrophobicity and to gain access to antigens potentially masked by the capsule was investigated. Treatment of capsulate or non-capsulate strains with the respective autologous antiserum resulted in a marked increase in surface hydrophobicity. Antisera raised against a rough non-capsulate (K) strain had little effect on the surface hydrophobicity of either of the capsulate strains K1O1 and K2 O1, or of the non-capsulate K O1 strain. Whereas anti-KO1 sera or anti-K2 sera increased the surface hydrophobicity of the K2 O1 strain, only antisera containing anti-K1 antibodies increased the hydrophobicity of the K1 O1 strain. Immunoadsorption of anti-KO1 serum by whole capsulate cells revealed that neither the K1 nor the K2 capsular polysaccharide acted as a barrier to anti-O antibodies but that the K1 capsular polysaccharide masked the presence of the immunoglobulin at the cell surface. The capsular polysaccharide does not appear to present a permeability barrier to immunoglobulins although failure to detect outer-membrane proteins in the immune complexes of either of the capsulate strains or of the KO1 strain suggests that the O antigen may prevent access of antibodies to these antigens.


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