Identification of lactoferrin-binding proteins from Treponema pallidum subspecies pallidum and Treponema denticola

Teanna M. Staggs, Margaret K. Greer, Joel B. Baseman, Stanley C. Holt, Victor V. Tryon

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Abstract

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 40 kDa 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 lactoferrin-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 languageEnglish (US)
Pages (from-to)613-619
Number of pages7
JournalMolecular Microbiology
Volume12
Issue number4
DOIs
StatePublished - May 1994

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Treponema denticola
Treponema pallidum
Lactoferrin
Globus Pallidus
Carrier Proteins
Proteins
Peptides
Phospholipase D
Spirochaetales
Competitive Binding
Syphilis
Transferrin
Affinity Chromatography
Detergents
Immune Sera

ASJC Scopus subject areas

  • Molecular Biology
  • Microbiology

Cite this

Identification of lactoferrin-binding proteins from Treponema pallidum subspecies pallidum and Treponema denticola. / Staggs, Teanna M.; Greer, Margaret K.; Baseman, Joel B.; Holt, Stanley C.; Tryon, Victor V.

In: Molecular Microbiology, Vol. 12, No. 4, 05.1994, p. 613-619.

Research output: Contribution to journalArticle

Staggs, Teanna M. ; Greer, Margaret K. ; Baseman, Joel B. ; Holt, Stanley C. ; Tryon, Victor V. / Identification of lactoferrin-binding proteins from Treponema pallidum subspecies pallidum and Treponema denticola. In: Molecular Microbiology. 1994 ; Vol. 12, No. 4. pp. 613-619.
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abstract = "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 40 kDa 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 lactoferrin-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.",
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