J. Busse et al., RECEPTOR AFFINITY PURIFICATION OF A LIPID-BINDING ADHESIN FROM HAEMOPHILUS-INFLUENZAE, The Journal of infectious diseases, 175(1), 1997, pp. 77-83
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.