A 16-kilodalton lipoprotein of the outer membrane of Serpulina (Treponema) hyodysenteriae.
Serpulina (Treponema) hyodysenteriae P18A and VS1 were extracted by using the detergent Triton X-114 and separated into detergent and aqueous phases. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western immunoblot analysis confirmed that a membrane-associated 16-kDa antigen was hydrophobic, since it was found in the detergent phase. A 45-kDa antigen partitioned into the aqueous phase, suggesting that it was hydrophilic and may be of periplasmic origin. When spirochetes were grown in the presence of [3H]palmitic acid, a predominant 16-kDa antigen was labeled; from the results of immunoprecipitation experiments, this antigen appeared to be the same as that recognized by both polyclonal and monoclonal antisera to a previously described 16-kDa antigen. This antigen was proteinase K sensitive and was not a component of the lipopolysaccharide, which, although [3H]palmitate labeled, was resistant to proteinase K digestion. The most probable explanation is that the 16-kDa antigen is a membrane-associated, surface-exposed, immunodominant lipoprotein.
Thomas
W
W
A.F.R.C. Institute for Animal Health, Compton, Berkshire, United Kingdom.
Sellwood
R
R
Lysons
R J
RJ
D000818:Animals; D001425:Bacterial Outer Membrane Proteins / Q000032:analysis* / Q000276:immunology; D001428:Bacterial Vaccines / Q000276:immunology; D015153:Blotting, Western; D004591:Electrophoresis, Polyacrylamide Gel; D019286:Endopeptidase K; D008074:Lipoproteins / Q000032:analysis* / Q000276:immunology; D019308:Palmitic Acid; D010169:Palmitic Acids / Q000378:metabolism; D012697:Serine Endopeptidases / Q000494:pharmacology; D013552:Swine; D014208:Treponema / Q000737:chemistry* / Q000276:immunology
D001425:Bacterial Outer Membrane Proteins; D001428:Bacterial Vaccines; D008074:Lipoproteins; D010169:Palmitic Acids; D019308:Palmitic Acid; D012697:Serine Endopeptidases; D019286:Endopeptidase K