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. 1984 Nov;46(2):598–607. doi: 10.1128/iai.46.2.598-607.1984

Purification and characterization of a cloned protease-resistant Treponema pallidum-specific antigen.

T E Fehniger, A M Walfield, T M Cunningham, J D Radolf, J N Miller, M A Lovett
PMCID: PMC261577  PMID: 6389353

Abstract

A cloned Treponema pallidum antigen, designated 4D, was purified from Escherichia coli predominantly as a 190-kilodalton (kd) polypeptide, although higher oligomeric forms exist. Extensive proteolysis of 4D created a limit digestion product of 90 kd which retained antigenicity with sera from patients with primary, secondary, early latent, late latent, and tertiary syphilis. A molecule indistinguishable from 90-kd 4D in size, isoelectric point, and antigenicity was isolated from T. pallidum after proteolysis. The 190- and 90-kd forms of 4D were stable at 68 degrees C but converted to 19- and 14-kd species, respectively, after boiling in sodium dodecyl sulfate. The low-molecular-weight species did not react with syphilitic sera. Rabbits immunized with the purified 4D antigen developed antibodies which immobilized virulent T. pallidum in a complement-dependent assay system, suggesting that the antigen has a native surface location.

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Selected References

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