The specificity and affinity of immunoliposome targeting to oral bacteria.

Immunoliposomes have been prepared using antibodies raised to an antigenic determinant on the cell surface of the oral bacterium Streptococcus oralis (S. oralis) in an investigation of their potential to reduce dental plaque. The N-succinimidyl-S-acetylthioacetate (SATA) derivative of the antibodies were conjugated through the reactive m-maleimidobenzoyl-N-hydroxysuccinimide (MBS) derivative of dipalmitoyl-phosphatidylethanolamine (DPPE) incorporated into liposomes. The degree of antibody conjugation to the liposomes was controlled by the percentage of DPPEMBS incorporated into the liposomes. The chemical modification of the antibodies did not affect the ability of the antibodies to bind to a S. oralis biofilm. However, the affinity of the immunoliposomes for S. oralis was much lower than that of the free antibody. The anti-oralis antibodies were highly specific for S. oralis. The anti-oralis immunoliposomes showed the greatest affinity for S. oralis, when targeted to a range of different oral bacterial biofilms. The immunoliposome targeting affinity for S. oralis was largely unaffected by the number of antibodies conjugated to the liposomal surface or by the net charge of the liposomal lipid bilayer. The immunoliposomes showed a greater affinity for S. oralis than 'naked' (bearing no antibody) liposomes. However, positively charged liposomes, incorporating stearylamine, adsorbed to S. oralis with greater affinities than the immunoliposomes. The immunoliposomes appeared to be physically stable over a period of 18 months, as judged by particle-size measurements.