Molecular characterization of the pathogen-specific, 34-kilodalton membrane immunogen of Treponema pallidum
نویسندگان
چکیده
منابع مشابه
Molecular characterization of the pathogen-specific, 34-kilodalton membrane immunogen of Treponema pallidum.
The 34-kilodalton (kDa) antigen of Treponema pallidum subsp. pallidum (T. pallidum) is a pathogen-specific integral membrane protein. DNA sequence analysis of the cloned gene revealed an open reading frame encoding a primary product of 204 residues with a molecular mass of 22,087 daltons. Sequences that correspond to a consensus Escherichia coli promoter and a ribosome-binding site were found u...
متن کاملMolecular cloning and characterization of the 15-kilodalton major immunogen of Treponema pallidum.
Pathogen-specific membrane immunogens of Treponema pallidum subsp. pallidum (T. pallidum) have been identified previously by phase partitioning with the nonionic detergent Triton X-114. One of these antigens, a 15-kilodalton (kDa) polypeptide, is expressed in relatively small quantities in T. pallidum but is highly immunogenic in both human and experimental syphilis. The native T. pallidum anti...
متن کاملSequence analysis of the 47-kilodalton major integral membrane immunogen of Treponema pallidum.
The complete primary amino acid sequence for the 47-kilodalton (kDa) major integral membrane immunogen of Treponema pallidum subsp. pallidum was obtained by using a combined strategy of DNA sequencing (of the cloned gene in Escherichia coli) and N-terminal amino acid sequencing of the native (T. pallidum subsp. pallidum-derived) antigen. An open reading frame believed to encode the 47-kDa antig...
متن کاملMolecular cloning and characterization of a 35.5-kilodalton lipoprotein of Treponema pallidum.
A clone expressing a 35.5-kDa recombinant treponemal protein was isolated from a genomic DNA library constructed from Treponema pallidum street strain 14. Polyclonal antiserum raised against the recombinant protein reacted with a corresponding native protein of comparable size in T. pallidum that is specific to the pathogenic treponemes. Radiolabeling of the recombinant protein with [3H]palmita...
متن کاملPorin activity and sequence analysis of a 31-kilodalton Treponema pallidum subsp. pallidum rare outer membrane protein (Tromp1).
We have recently reported the isolation and purification of the Treponema pallidum outer membrane and the identification of its rare protein constituents, including a 31-kDa protein markedly enriched in the outer membrane preparation (D.R. Blanco, K. Reimann, J. Skare, C.I. Champion, D. Foley, M. M. Exner, R. E. W. Hancock, J. N. Miller, and M. A. Lovett, J. Bacteriol. 176:6088-6099, 1994). In ...
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ژورنال
عنوان ژورنال: Infection and Immunity
سال: 1989
ISSN: 0019-9567,1098-5522
DOI: 10.1128/iai.57.11.3314-3323.1989