The outer membrane, not a coat of host proteins, limits antigenicity of virulent Treponema pallidum.
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Syphilis: the renaissance of an old disease with oral implicationsSyphilis: review with emphasis on clinical, epidemiologic, and some biologic featuresSpirochaetal lipoproteins and pathogenesisStructural and Biochemical Basis for Polyamine Binding to the Tp0655 Lipoprotein of Treponema pallidum: Putative Role for Tp0655 (TpPotD) as a Polyamine ReceptorFactors determining human-to-human transmissibility of zoonotic pathogens via contactBipartite Topology of Treponema pallidum Repeat Proteins C/D and I: OUTER MEMBRANE INSERTION, TRIMERIZATION, AND PORIN FUNCTION REQUIRE A C-TERMINAL β-BARREL DOMAINThe major outer sheath protein (Msp) of Treponema denticola has a bipartite domain architecture and exists as periplasmic and outer membrane-spanning conformersSurface immunolabeling and consensus computational framework to identify candidate rare outer membrane proteins of Treponema pallidum.Cryo-electron tomography elucidates the molecular architecture of Treponema pallidum, the syphilis spirocheteIdentification of a Treponema denticola OppA homologue that binds host proteins present in the subgingival environmentTreponema pallidum major sheath protein homologue Tpr K is a target of opsonic antibody and the protective immune response.Characterization and serologic analysis of the Treponema pallidum proteome.Lipid modification of the 17-kilodalton membrane immunogen of Treponema pallidum determines macrophage activation as well as amphiphilicity.Cellular architecture of Treponema pallidum: novel flagellum, periplasmic cone, and cell envelope as revealed by cryo electron tomography.Bifunctional role of the Treponema pallidum extracellular matrix binding adhesin Tp0751.Membrane topology and cellular location of the Treponema pallidum glycerophosphodiester phosphodiesterase (GlpQ) ortholog.The Treponema denticola major sheath protein is predominantly periplasmic and has only limited surface exposure.Lack of humoral immune protection against Treponema denticola virulence in a murine modelThe tprK gene is heterogeneous among Treponema pallidum strains and has multiple allelesBiological basis for syphilis.Opsonization of Treponema pallidum is mediated by immunoglobulin G antibodies induced only by pathogenic treponemes.Virulent Treponema pallidum promotes adhesion of leukocytes to human vascular endothelial cells.Dermal inflammation elicited by synthetic analogs of Treponema pallidum and Borrelia burgdorferi lipoproteins.The rare outer membrane protein, OmpL1, of pathogenic Leptospira species is a heat-modifiable porin.Characterization of outer membranes isolated from Treponema pallidum, the syphilis spirocheteMolecular cloning and sequence analysis of the gene encoding LipL41, a surface-exposed lipoprotein of pathogenic Leptospira speciesCharacterization of the low-molecular-mass proteins of virulent Treponema pallidum.Identification and characterization of the Treponema pallidum tpn50 gene, an ompA homologSimilarity between the 38-kilodalton lipoprotein of Treponema pallidum and the glucose/galactose-binding (MglB) protein of Escherichia coli.Outer membrane proteins of pathogenic spirochetes.The 47-kDa major lipoprotein immunogen of Treponema pallidum is a penicillin-binding protein with carboxypeptidase activityIsolation of the outer membranes from Treponema pallidum and Treponema vincentii.Analysis of Borrelia burgdorferi membrane architecture by freeze-fracture electron microscopyTreponema pallidum rare outer membrane proteins: analysis of mobility by freeze-fracture electron microscopy.The Tp0684 (MglB-2) Lipoprotein of Treponema pallidum: A Glucose-Binding Protein with Divergent Topology.The TprK protein of Treponema pallidum is periplasmic and is not a target of opsonic antibody or protective immunity.Treponema pallidum Lipoprotein TP0435 Expressed in Borrelia burgdorferi Produces Multiple Surface/Periplasmic Isoforms and mediates Adherence.Polypeptides of Treponema pallidum: progress toward understanding their structural, functional, and immunologic roles. Treponema Pallidum Polypeptide Research Group.Spirochetal Lipoproteins and Immune Evasion.The Cross-Talk between Spirochetal Lipoproteins and Immunity.
P2860
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P2860
The outer membrane, not a coat of host proteins, limits antigenicity of virulent Treponema pallidum.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
The outer membrane, not a coat ...... f virulent Treponema pallidum.
@en
type
label
The outer membrane, not a coat ...... f virulent Treponema pallidum.
@en
prefLabel
The outer membrane, not a coat ...... f virulent Treponema pallidum.
@en
P2093
P2860
P1476
The outer membrane, not a coat ...... f virulent Treponema pallidum.
@en
P2093
P2860
P304
P407
P577
1992-03-01T00:00:00Z