The Toll-like Receptor Protein Rp105 Regulates Lipopolysaccharide Signaling in B Cells

Ogata, Hirotaka; Su, I-hsin; Miyake, Kensuke; Nagai, Yoshinori; Akashi, Shigeo; Mecklenbräuker, Ingrid; Rajewsky, Klaus; Kimoto, Masao; Tarakhovsky, Alexander

doi:10.1084/jem.192.1.23

Cited by 273 publications

(238 citation statements)

References 24 publications

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“…In contrast, they found normal levels of surface expression of Rp105, an orphan Toll-like receptor, but cross-linking failed to induce B cell proliferation even though 129/Sv B cells proliferated in response to LPS (50). These findings are in apparent contradiction with recent data demonstrating reduced LPS-mediated proliferation of B cells in mice lacking Rp105 (51). Perhaps, Corcoran and Metcalf's (50) data is a reflection of a polymorphism in 129-derived Rp105 that renders the stimulating Ab ineffective in this strain.…”

Section: Discussioncontrasting

confidence: 78%

Aberrant DAP12 Signaling in the 129 Strain of Mice: Implications for the Analysis of Gene-Targeted Mice

McVicar

Winkler‐Pickett

Taylor

et al. 2002

The Journal of Immunology

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NK cells are implicated in antiviral responses, bone marrow transplantation and tumor immunosurveillance. Their function is controlled, in part, through the Ly49 family of class I binding receptors. Inhibitory Ly49s suppress signaling, while activating Ly49s (i.e., Ly49D) activate NK cells via the DAP12 signaling chain. Activating Ly49 signaling has been studied primarily in C57BL/6 mice, however, 129 substrains are commonly used in gene-targeting experiments. In this study, we show that in contrast to C57BL/6 NK cells, cross-linking of DAP12-coupled receptors in 129/J mice induces phosphorylation of DAP12 but not calcium mobilization or cytokine production. Consistent with poor-activating Ly49 function, 129/J mice reject bone marrow less efficiently than C57BL/6 mice. Sequence analysis of receptors and DAP12 suggests no structural basis for inactivity, and both the 129/J and C57BL/6 receptors demonstrate normal function in a reconstituted receptor system. Most importantly, reconstitution of Ly49D in 129/J NK cells demonstrated that the signaling deficit is within the NK cells themselves. These unexpected findings bring into question any NK analysis of 129/J, 129Sv, or gene-targeted mice derived from these strains before complete backcrossing, and provide a possible explanation for the differences observed in the immune response of 129 mice in a variety of models.

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Section: Discussioncontrasting

confidence: 78%

Aberrant DAP12 Signaling in the 129 Strain of Mice: Implications for the Analysis of Gene-Targeted Mice

McVicar

Winkler‐Pickett

Taylor

et al. 2002

The Journal of Immunology

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“…Shown are mean Ϯ SEM (ng/ml) of the IL-8 concentration in three transfected wells. recent study of RP105, a transmembrane molecule with extracellular domain similarity to TLRs (42), demonstrated functional cooperation between RP105 and TLR4 on cotransfection of these molecules into Ba/F3 cells. Thus, comparison with closely related receptor systems suggests that TLR1-TLR2 heterodimerization is the most likely explanation for the phenomenon described here, although we do not show whether this occurs directly or indirectly.…”

Section: Discussionmentioning

confidence: 99%

Evidence for an Accessory Protein Function for Toll-Like Receptor 1 in Anti-Bacterial Responses

Wyllie

Kiss-Tóth

Visintin

et al. 2000

The Journal of Immunology

245

151

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Members of the Toll-like receptor (TLR) family are components of the mammalian anti-microbial response, signaling with a domain closely related to that of IL-1 receptors. In this report the expression and function of TLR1, a TLR of unknown function, are examined. TLR1 is expressed by monocytes, as demonstrated using a novel mAb. Monocytes also express TLR2. TLR1 transfection of HeLa cells, which express neither TLR1 nor TLR2, was not sufficient to confer responsiveness to several microbial extracts. However, cotransfection of TLR1 and TLR2 resulted in enhanced signaling by HeLa cells to soluble factors released from Neisseria meningitidis relative to the response with either TLR alone. This phenomenon was also seen with high concentrations of some preparations of LPS. The N. meningitidis factors recognized by TLR1/TLR2 were not released by N. meningitidis mutant in the LpxA gene. Although LpxA is required for LPS biosynthesis, because cooperation between TLR1 and TLR2 was not seen with all LPS preparations, the microbial component(s) TLR1/2 recognizes is likely to be a complex of LPS and other molecules or a compound metabolically and chemically related to LPS. The functional IL-1R consists of a heterodimer; this report suggests a similar mechanism for TLR1 and TLR2, for certain agonists. These data further suggest that mammalian responsiveness to some bacterial products may be mediated by combinations of TLRs, suggesting a mechanism for diversifying the repertoire of Toll-mediated responses.

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“…TLR2 -/-, TLR4 -/-, MyD88 -/-, TRIF -/-, RP105 -/-and MD-2 -/-mice of the strain C57BL/6 [7,[19][20][21][22] were bred and maintained under specific pathogen-free conditions at the Animal Center, Institute of Medical Science, University of Tokyo. C57BL/6 (WT) mice were purchased from Japan SLC (Hamamatsu, Japan).…”

Section: Experimental Animals and Pba Infectionmentioning

confidence: 99%

Mast cell‐mediated immune responses through IgE antibody and Toll‐like receptor 4 by malarial peroxiredoxin

et al. 2008

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In this study, 2-Cys Plasmodium berghei ANKA (PbA) peroxiredoxin (Prx) was identified as an antigenic protein recognized by an anti-PbA IgE antibody using two-dimensional polyacrylamide gel electrophoresis and proteomic analysis. Innate immune responses to PbAPrx were examined using cells from mice deficient in Toll-like receptors (TLR) or related molecules, and it was demonstrated that responses were severely impaired in TLR4 -/-, MyD88 -/-and MD-2 -/-mice, but not in Toll/IL-1 receptor domain-containing adaptor inducing IFN-c (TRIF) -/-, TLR2 -/-or radioprotective 105 (RP105) -/-mice. An association between PbAPrx and TLR4 was observed following immunoprecipitation and immunoblotting, suggesting that PbAPrx was associated with TLR4/MD-2. Interactions between Prx and TLR4/MD-2 were also examined by flow cytometry using TLR4/MD-2-or TLR2-expressing cells. NFjB/GFP activity was observed in TLR4/MD-2-but not in TLR2-expressing cells following stimulation with Prx. However, this effect was not observed after treatment with proteinase K, suggesting that PbAPrx is a protein ligand for TLR4 and that the PbAPrx activity observed in this study is not due to contamination with LPS. These findings indicate that malarial Prx induces IgE-mediated protection through FceRI on mast cells and innate immunity through TLR4 with MyD88 and MD-2, suggesting a novel function for malarial Prx in innate and acquired immune responses in malaria.

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The Toll-like Receptor Protein Rp105 Regulates Lipopolysaccharide Signaling in B Cells

Cited by 273 publications

References 24 publications

Aberrant DAP12 Signaling in the 129 Strain of Mice: Implications for the Analysis of Gene-Targeted Mice

Aberrant DAP12 Signaling in the 129 Strain of Mice: Implications for the Analysis of Gene-Targeted Mice

Evidence for an Accessory Protein Function for Toll-Like Receptor 1 in Anti-Bacterial Responses

Mast cell‐mediated immune responses through IgE antibody and Toll‐like receptor 4 by malarial peroxiredoxin

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