Major integral membrane protein immunogens of Treponema pallidum are proteolipids

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Sequence analysis of the 47-kilodalton major integral membrane immunogen of Treponema pallidum.

The complete primary amino acid sequence for the 47-kilodalton (kDa) major integral membrane immunogen of Treponema pallidum subsp. pallidum was obtained by using a combined strategy of DNA sequencing (of the cloned gene in Escherichia coli) and N-terminal amino acid sequencing of the native (T. pallidum subsp. pallidum-derived) antigen. An open reading frame believed to encode the 47-kDa antig...

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TP0453, a concealed outer membrane protein of Treponema pallidum, enhances membrane permeability.

The outer membrane of Treponema pallidum, the non-cultivable agent of venereal syphilis, contains a paucity of protein(s) which has yet to be definitively identified. In contrast, the outer membranes of gram-negative bacteria contain abundant immunogenic membrane-spanning beta-barrel proteins mainly involved in nutrient transport. The absence of orthologs of gram-negative porins and outer membr...

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Molecular characterization of receptor binding proteins and immunogens of virulent Treponema pallidum

Receptor binding proteins of Treponema pallidum were identified by incubation of [35S]methionine-labeled, soluble T. pallidum preparations with formaldehyde-fixed HEp-2 cells. Three major treponemal proteins (bands 1--3) that avidly bound to the eucaryotic cell surface were detected by sodium dodecylsulfate-polyacrylamide gel electrophoresis and fluorography. Brief trypsin treatment of HEp-2 ce...

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Shape of Treponema pallidum.

Treponema pallidum was found to be not helical, but a flat wave twisted into one to five different planes per cell.

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Mucopolysaccharidase of Treponema pallidum.

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ژورنال

عنوان ژورنال: Infection and Immunity

سال: 1989

ISSN: 0019-9567,1098-5522

DOI: 10.1128/iai.57.9.2872-2877.1989