Major integral membrane protein immunogens of Treponema pallidum are proteolipids
- Univ. of Texas Southwestern Medical Center, Dallas (USA)
A number of the major pathogen-specific immunogens of Treponema pallidum were characterized recently as amphiphilic, integral membrane proteins by phase partitioning with Triton X-114. In the present study, we demonstrated that the same membrane immunogens (designated as detergent phase proteins (DPPs)) become radiolabeled upon in vitro incubation of T. pallidum with various {sup 3}H-labeled fatty acids. Radioimmunoprecipitation with a monoclonal antibody confirmed that the {sup 3}H-labeled 47-kilodalton protein corresponded to the well-characterized treponemal antigen with the identical apparent molecular mass. Failure to detect {sup 3}H-labeled DPPs following incubation with erythromycin confirmed that protein acylation required de novo protein synthesis by the bacteria. When treponemes were incubated with ({sup 3}H)myristate, ({sup 3}H)palmitate, or ({sup 3}H)oleate, radiolabeled proteins corresponding to the DPPs were detected upon autoradiography. Demonstration that a number of the abundant membrane immunogens of T. pallidum are proteolipids provides information to help clarify their membrane association(s) and may serve to explain their extraordinary immunogenicity.
- OSTI ID:
- 5132087
- Journal Information:
- Infection and Immunity; (USA), Journal Name: Infection and Immunity; (USA) Vol. 57:9; ISSN 0019-9567; ISSN INFIB
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
59 BASIC BIOLOGICAL SCIENCES
ANIMALS
ANTIGENS
AUTORADIOGRAPHY
BACTERIA
BIOASSAY
CARBOXYLIC ACIDS
CHEMICAL COMPOSITION
DIAGNOSTIC TECHNIQUES
HYDROGEN COMPOUNDS
IMMUNOASSAY
IMMUNOLOGY
ISOTOPE APPLICATIONS
LIPIDS
LIPOPROTEINS
MAMMALS
MEMBRANE PROTEINS
MEMBRANES
MICROORGANISMS
ORGANIC ACIDS
ORGANIC COMPOUNDS
PROTEINS
RABBITS
RADIOASSAY
RADIOIMMUNOASSAY
RADIOIMMUNODETECTION
RADIOIMMUNOLOGY
STRUCTURE-ACTIVITY RELATIONSHIPS
TRACER TECHNIQUES
TRITIUM COMPOUNDS
VERTEBRATES