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Porin activity of the native and recombinant outer membrane protein Oms28 of Borrelia burgdorferi
It is confirmed that Oms28 is a B. burgdorferi porin, the first to be described, with potential relevance to the pathogenesis of Lyme borreliosis and to the physiology of the spirochete.
Virulent strain associated outer membrane proteins of Borrelia burgdorferi.
Using antiserum with specificity for virulent strain B31, OMV antigens on the surface of the spirochete are identified and proteins whose presence in OMV could be correlated with virulence and protective immunity in the rabbit Lyme disease model.
Selective release of the Treponema pallidum outer membrane and associated polypeptides with Triton X-114
Results indicate that 1% Triton X-114 selectively solubilizes the T. pallidum outer membrane and associated proteins of likely outer membrane location.
Isolation and characterization of the outer membrane of Borrelia hermsii.
The purification of outer membrane vesicles (OMV) from B. hermsii HS-1 and the subsequent identification and characterization of their constituent outer membrane proteins should aid in further studies of pathogenesis and immunity of tick-borne relapsing fever.
Molecular cloning and sequence analysis of the gene encoding OmpL1, a transmembrane outer membrane protein of pathogenic Leptospira spp
DNA hybridization studies indicate that the ompL1 gene is present in a single copy in all pathogenic Leptospira species that have been tested and is absent in nonpathogenic Lepsira species.
Immunity in experimental syphilis. VI. Successful vaccination of rabbits with Treponema pallidum, Nichols strain, attenuated by -irradiation.
  • J. N. Miller
  • Biology, Medicine
    Journal of immunology
  • 1 May 1973
Conclusive evidence that TPI antibody is not associated with the immune response was provided by the finding that 8 of the 11 immune rabbits challenged 1 year after vaccination had no TPI antibodies before challenge and failed to develop immobilizing antibody during the 3-month period of observation after challenge.
Attachment of Treponema pallidum to fibronectin, laminin, collagen IV, and collagen I, and blockage of attachment by immune rabbit IgG.
The IgG from immune serum blocked treponemal attachment to the cultured cells and to fibronectin, laminin, collagen IV, and collagen I, but not to hyaluronic acid, which is a major component of basement membranes and extracellular matrices.
The Oms66 (p66) protein is a Borrelia burgdorferi porin
In this study we report the purification and characterization of a 66-kDa protein, designated Oms66, for outer membrane-spanning 66-kDa protein, that functions as a porin in the outer membrane (OM)
Cloning, sequencing, and expression of two class B endoflagellar genes of Treponema pallidum subsp. pallidum encoding the 34.5- and 31.0-kilodalton proteins
Two structural endoflagellar genes of Treponema pallidum that encode the 34.5- and 31.0-kilodalton polypeptides as detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis were cloned, sequenced, and expressed and revealed fusion proteins having molecular masses of 61.0 and 59.0 kDa.
Humoral immune response in human syphilis to polypeptides of Treponema pallidum.
The results suggest that a correlation exists between acquisition of antibody and the development of "chancre immunity" and the loss of antibody that characterizes late latent and late syphilis may be associated with the potential development of destructiveLate syphilis.