Receptor Affinity Purification of a Lipid-Binding Adhesin from Haemophilus influenzae
Open Access
- 1 January 1997
- journal article
- Published by Oxford University Press (OUP) in The Journal of Infectious Diseases
- Vol. 175 (1) , 77-83
- https://doi.org/10.1093/infdis/175.1.77
Abstract
Thirteen clinical strains of Haemophilus influenzae, including types b, d, and untypeable, in vitro specifically recognize phosphatidylethanolamine (PE), gangliotetraosylceramide, gangliotriosylceramide (Gg3), sulfatoxygalactosylceramide, and to a lesser extent sulfatoxygalactosylglycerol. A PE affinity matrix was used to purify an adhesin of ∼46 kDa from both type band untypeable H. influenzae. This adhesin was a potent inhibitor of H. influenzae Gg3 and PE binding in vitro, and polyclonal antibodies specific for this protein prevented the attachment of H. influenzae Gg3 and PE and cultured HEp-2 epithelial cells in vitro.Keywords
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