Molecular cloning of Treponema pallidum outer envelope fibronectin binding proteins, P1 and P2

Kenneth Peterson, Joel B. Baseman, John F. Alderete

Research output: Contribution to journalArticle

9 Scopus citations

Abstract

Phages directing the synthesis of Treponema pallidum fibronectin binding adhesin proteins, P1 and P2,1 were isolated from an EMBL-3 bacteriophage lambda library of T pallidum deoxyribonucleic acid (DNA). The recombinant phages were identified using antisera generated to treponemal proteins purified in fibronectin-Sepharose. Recombinant P1 and P2 proteins possessed the same relative molecular weights as the native surface polypeptides of spirochaetes. The structural genes for these proteins were subcloned into the plasmid vector pUC19, and transformed Escherichia coli expressed and translocated recombinant P1 and P2 to their outer membranes. Finally, the recombinant adhesin proteins, P1 and P2, were purified from detergent solubilised E coli outer membrane preparations using fibronectin-Sepharose affinity chromatography, which confirmed that the fibronectin binding properties of the cloned proteins were retained.

Original languageEnglish (US)
Pages (from-to)355-360
Number of pages6
JournalSexually Transmitted Infections
Volume63
Issue number6
DOIs
StatePublished - 1987

ASJC Scopus subject areas

  • Dermatology
  • Infectious Diseases

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