RECEPTOR AFFINITY PURIFICATION OF A LIPID-BINDING ADHESIN FROM HAEMOPHILUS-INFLUENZAE

Thirteen clinical strains of Haemophilus influenzae, including types b , d, and untypeable, in vitro specifically recognize phosphatidylethan olamine (PE), gangliotetraosylceramide, gangliotriosylceramide (Gg(3)) , sulfatoxygalactosylceramide, and to a lesser extent sulfatoxygalacto sylglycerol. A PE affinity matrix was used to purify an adhesin of sim ilar to 46 kDa from both type b and untypeable H. influenzae. This adh esin was a potent inhibitor of H. influenzae Gg(3) and PE binding in v itro, and polyclonal antibodies specific for this protein prevented th e attachment of H. influenzae Gg(3) and PE and cultured HEp-2 epitheli al cells in vitro.