Pathogen specificity of Treponema pallidum subsp. pallidum integral membrane proteins identified by phase partitioning with Triton X-114.
The antigenically conserved proteins of Treponema pallidum subsp. pallidum and four nonpathogenic cultivatable treponemes were investigated by phase partitioning with the nonionic detergent Triton X-114 and immunoblot analysis. None of the T. pallidum integral membrane proteins identified by phase partitioning (detergent-phase proteins) appeared to be antigenically related to proteins of the nonpathogens. Protease-resistant material similar to lipopolysaccharide was identified in the detergent phase from T. phagedenis biotype Reiter but was not detected in T. pallidum.
Radolf
J D
JD
Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas 75235.
Norgard
M V
MV
D000818:Animals; D000942:Antigens, Bacterial / Q000302:isolation & purification*; D002498:Centrifugation; D003902:Detergents; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007118:Immunoassay; D008297:Male; D008565:Membrane Proteins / Q000276:immunology / Q000302:isolation & purification*; D017830:Octoxynol; D011092:Polyethylene Glycols; D011817:Rabbits; D013501:Surface-Active Agents; D014210:Treponema pallidum / Q000032:analysis / Q000276:immunology / Q000472:pathogenicity*
D000942:Antigens, Bacterial; D003902:Detergents; D008565:Membrane Proteins; D013501:Surface-Active Agents; D011092:Polyethylene Glycols; D017830:Octoxynol; C010615:Nonidet P-40