Lactoferrin‐binding or ‐associated proteins were identified in Treponema pallidum subspecies pallidum and Treponema denticola by affinity column chromatography using human lactoferrin and detergent‐solubilized, radiolabelled spirochaetes. Two discrete polypeptides of T. pallidum with masses of 45 and 40kDa and a broad band from 29‐34 kDa exhibited association with human apo‐ and partially ferrated lactoferrin. T. denticola produced two proteins that associated with a lactoferrin affinity matrix (50 and 35 kDa). T. pallidum and T. denticola did not associate with soluble, human transferrin in parallel experiments. Soluble human lactoferrin competed with all lactoferrin‐associated proteins from T. pallidum and T. denticola in competitive‐binding assays. However, the T. denticola proteins dissociated from a lacto‐ferrin‐affinity matrix in the presence of differing concentrations of unlabelled, soluble lactoferrin competitor. Treatment with phospholipase D altered migration of the diffuse 29‐34 kDa band of T. pallidum suggesting that the polypeptide was lipid‐modified. Each of the lactoferrin‐binding proteins from T. pallidum and T. denticola reacted with pooled rabbit syphilitic antisera. The lactoferrin‐binding proteins of T. pallidum reacted with human sera from patients at all stages of syphilis. In addition, a monoclonal antibody generated against the 45 kDa polypeptide of T. pallidum crossreacted with the 29–34 kDa protein.
|Original language||English (US)|
|Number of pages||7|
|State||Published - May 1994|
ASJC Scopus subject areas
- Molecular Biology