Identification of outer membrane proteins of Bartonella bacilliformis.
Purification of the outer membrane of Bartonella bacilliformis by sucrose step gradient centrifugation and analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) suggest that 14 proteins, ranging from 11.2 to 75.3 kDa, are located in the outer membrane of the pathogen. On the basis of M(r)s, eleven of these proteins have counterparts which are labeled by extrinsic radioiodination of intact bartonellae, and two of the proteins are visibly sensitive to extrinsic proteinase K digestion in analysis by SDS-PAGE. While nearly all the extrinsically radioiodinated proteins could be immunoprecipitated with rabbit antibartonella hyperimmune serum, proteins of 31.5, 42, and 45 kDa were prominent immunoprecipitants. Purified lipopolysaccharide from the outer membrane of B. bacilliformis produced a diffuse band of approximately 5 kDa on SDS-PAGE and was not detectable on immunoblots developed with rabbit antibartonella hyperimmune antiserum.
Minnick
M F
MF
Division of Biological Sciences, University of Montana, Missoula 59812-1002.
D001425:Bacterial Outer Membrane Proteins / Q000302:isolation & purification*; D001473:Bartonella / Q000737:chemistry*; D019286:Endopeptidase K; D008070:Lipopolysaccharides / Q000302:isolation & purification; D011233:Precipitin Tests; D012697:Serine Endopeptidases / Q000494:pharmacology
D001425:Bacterial Outer Membrane Proteins; D008070:Lipopolysaccharides; D012697:Serine Endopeptidases; D019286:Endopeptidase K