PMID:27161310

Citation	Chan, K, Nasereddin, T, Alter, L, Centurion-Lara, A, Giacani, L and Parveen, N (2016) Treponema pallidum Lipoprotein TP0435 Expressed in Borrelia burgdorferi Produces Multiple Surface/Periplasmic Isoforms and mediates Adherence. Sci Rep 6:25593
Abstract	The ability of Treponema pallidum, the syphilis spirochete to colonize various tissues requires the presence of surface-exposed adhesins that have been difficult to identify due to the inability to culture and genetically manipulate T. pallidum. Using a Borrelia burgdorferi-based heterologous system and gain-in-function approach, we show for the first time that a highly immunogenic lipoprotein TP0435 can be differentially processed into multiple isoforms with one variant stochastically displayed on the spirochete surface. TP0435 was previously believed to be exclusively located in T. pallidum periplasm. Furthermore, non-adherent B. burgdorferi strain expressing TP0435 acquires the ability to bind to a variety of host cells including placental cells and exhibits slow opsonophagocytosis in vitro similar to poor ex vivo phagocytosis of T. pallidum by host macrophages reported previously. This phenomenon of production of both surface and periplasmic immunogenic lipoprotein isoforms has possible implications in immune evasion of the obligate pathogen T. pallidum during infection.
Links	PubMed PMC4861935 Online version:10.1038/srep25593
Keywords	Animals; Bacterial Adhesion/genetics; Bacterial Adhesion/immunology; Bacterial Proteins/genetics; Bacterial Proteins/immunology; Bacterial Proteins/metabolism; Borrelia burgdorferi/genetics; Borrelia burgdorferi/immunology; Borrelia burgdorferi/metabolism; Carrier Proteins/genetics; Carrier Proteins/immunology; Carrier Proteins/metabolism; Cell Line; Cell Line, Tumor; HEK293 Cells; Humans; Lipoproteins/genetics; Lipoproteins/immunology; Lipoproteins/metabolism; Macrophages/immunology; Macrophages/metabolism; Macrophages/microbiology; Membrane Proteins/genetics; Membrane Proteins/immunology; Membrane Proteins/metabolism; Mice, Inbred BALB C; Periplasm/immunology; Periplasm/metabolism; Phagocytosis/immunology; Protein Isoforms/genetics; Protein Isoforms/immunology; Protein Isoforms/metabolism; Transgenes/genetics; Transgenes/immunology; Treponema pallidum/genetics; Treponema pallidum/immunology; Treponema pallidum/metabolism
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
TREPA:TA17	Colocalizes with	GO:0005886: plasma membrane	ECO:0005592: immunogold labelling electron microscopy assay evidence used in manual assertion		C		In Figure 3, Immuno-SEM, specifically using immunogold labeling, was utilized to analyze the position of TP0435 (also known as gene tpp17) on the plasma membrane. There was not much gold/antibiotic tagging when the outside of the B. burgdorferi cell was labeled. In Figure 4, immunogold labeling was utilized again to show that the tpp17 structural protein is much more present in the inner, periplasmic side of the outer plasma membrane of the B. burgdorferi cell.	complete CACAO 13555
TREPA:TA17	Colocalizes with	GO:0005886: plasma membrane	ECO:0007103: epitope-tagged protein immunolocalization evidence used in manual assertion		C		Figure 1 displays the results of Indirect Flourescent Antibody assays (IFA) conducted on two B. burgdorferi strains, one containing an empty vector and the other containing a TP0435 vector. In columns A and C, the surfaces of both strains were stained while in columns B and D, the membranes of both strains were permeabilized before staining. Both vector strains were labeled more frequently than the control strains, indicating that the addition of the vector resulted in the expression of TP0435. In addition, permeabilization of the vector strain membrane resulted in significantly more staining than the nonpermeable vector strain, indicating that TP0435 was more frequently present on the periplasmic membrane surface.	complete CACAO 13649

References

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