Characterization of outer membrane and secreted proteins of Leptospira interrogans serovar pomona

Microb Pathog. 1991 Apr;10(4):311-22. doi: 10.1016/0882-4010(91)90014-2.


Outer membrane and secreted proteins were isolated from Leptospira interrogans serovar pomona and characterized by sodium dodecyl sulfate polyacrylamide gel electrophoresis, immunoblot and radioimmunoprecipitation techniques. The L. interrogans outer membranes were extracted with Triton X-114 and contained several proteins. The major cellular protein with a molecular mass of 31 kDa was associated exclusively with the L. interrogans outer membrane. Using a whole cell immunoprecipitation method, five hydrophobic, Triton X-114 extractable proteins (22, 26, 31, 36 and 42 kDa) were exposed on the surface of L. interrogans. The 31 kDa protein was heat labile and was a potent antigen in animals experimentally infected with L. interrogans serovar pomona. Several proteins were secreted by L. interrogans including a 60 kDa protein tentatively identified as the L. interrogans hemolysin.

MeSH terms

  • Animals
  • Bacterial Outer Membrane Proteins / analysis*
  • Bacterial Outer Membrane Proteins / immunology
  • Bacterial Proteins / metabolism*
  • Hemolysin Proteins / analysis
  • Hemolysin Proteins / immunology
  • Hemolysin Proteins / metabolism
  • Hot Temperature
  • Leptospira interrogans / analysis*
  • Leptospira interrogans / growth & development
  • Leptospira interrogans / metabolism
  • Membrane Proteins / isolation & purification
  • Molecular Weight
  • Swine


  • Bacterial Outer Membrane Proteins
  • Bacterial Proteins
  • Hemolysin Proteins
  • Membrane Proteins