Affinities of Treponema pallidum for human lactoferrin and transferrin

J. F. Alderete, K. M. Peterson, J. B. Baseman

Research output: Contribution to journalArticle

22 Scopus citations

Abstract

The acquisition of lactoferrin and transferrin by live Treponema pallidum organisms was examined. Saturation binding kinetics were obtained for virulent treponemes with increasing amounts of radioiodinated lactoferrin but not with transferrin. Furthermore, lactoferrin bound up to 100 times more effectively than transferrin. Only unlabelled lactoferrin stoichiometrically competed with iodinated lactoferrin binding. Time course kinetics showed maximum lactoferrin acquisition within the first five minutes at 34°C. Optimum iron accumulation, however, was achieved by Tpallidum in 30 minutes at 34°C, and amounts of iron were six times greater than the equivalent amount of lactoferrin bound. Interestingly, iron uptake was also detected in the presence of transferrin, despite the minimal amounts of transferrin acquired by live treponemes. These observations reinforce the possibility that the associations of Tpallidum with host molecules, such as plasma proteins, are essential for survival of the parasite within host environments.

Original languageEnglish (US)
Pages (from-to)359-363
Number of pages5
JournalSexually Transmitted Infections
Volume64
Issue number6
DOIs
StatePublished - Jan 1 1988

    Fingerprint

ASJC Scopus subject areas

  • Dermatology
  • Infectious Diseases

Cite this