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Proximity labeling and identification of the proteins that interact with Siglec-14 on THP-1 cells

ABSTRACT: Proteins that interact with Siglec-14 were identified by proximity labeling, followed by streptavidin affinity purification and proteomic analysis. MaxQuant software was used for the quantitative analysis of the proteins identified.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Monocyte, Cell Culture

SUBMITTER: Jimmy Huang

LAB HEAD: Takashi Angata

PROVIDER: PXD009748 | Pride | 2018-11-04

REPOSITORIES: Pride

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Soluble Siglec-14 glycan-recognition protein is generated by alternative splicing and suppresses myeloid inflammatory responses.

Huang Po-Chun Jimmy PJ Low Penk-Yeir PY Wang Iren I Hsu Shang-Te Danny SD Angata Takashi T

The Journal of biological chemistry 20181030 51

Human sialic acid-binding immunoglobulin-like lectin 14 (Siglec-14) is a glycan-recognition protein that is expressed on myeloid cells, recognizes bacterial pathogens, and elicits pro-inflammatory responses. Although Siglec-14 is a transmembrane protein, a soluble form of Siglec-14 is also present in human blood. However, the mechanism that generates soluble Siglec-14 and what role this protein form may play remain unknown. Here, investigating the generation and function of soluble Siglec-14, we ...[more]

PMID: 30377253

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Identification of Siglec-7-ligand candidates on JVM-3 human B cell line by proximity labeling

Project description:Siglec-7 is a member of Siglec family of glycan recognition proteins involved in the regulation of natural killer (NK) cell activities. We found Siglec-7 ligand is highly expressed on JVM-3, a B cell chronic lymphocytic leukemia (B-CLL) cell line. In this experiment, we attempted at identifying the ligands of Siglec-7 on JVM-3 by applying the proximity labeling method we developed (Chang L et al., J Proteome Res. 2017, 16:3929-41).

2022-05-31 | PXD024690 | Pride

Identification of Siglec-E-ligand candidates on BCL-1 mouse B cell line by proximity labeling

Project description:Siglec-E is a member of Siglec family of glycan recognition proteins involved in the regulation of myeloid cell activities. Siglec-E preferentially recognizes disialic acid, a glycan epitope consisting of two sialic acids conjugated in alpha2-8 linkage (Zhang JQ et al., Eur J Immunol. 2004, 34:1175-84). BCL-1, a mouse B cell line, expresses disialic acid epitope (Wang SH et al., Glycobiology. 2013, 23:677-89). In this experiment, we attempted at identifying the ligands of Siglec-E on BCL-1 by applying the proximity labeling method we developed (Chang L et al., J Proteome Res. 2017, 16:3929-41).

2022-02-25 | PXD013032 | Pride

Identification of Siglec ligands in human B cell

Project description:Siglecs are a family of receptor-type glycan recognition proteins (lectins) involved in self - nonself discrimination by the immune system. Identification of Siglec ligand(s) is necessary to understand how Siglec-ligand interaction translates to biological outcomes, but is challenging because the interaction is weak. To facilitate identification of Siglec ligands, we adopted proximity labeling method based on tyramide radicalization principle.

2017-09-29 | PXD006359 | Pride

Structural insights into Siglec-15 reveal glycosylation dependency for its interaction with T cells through integrin CD11b

Project description:Sialic acid-binding Ig-like lectin 15 (Siglec-15) is emerging as an immune modulator and target for cancer immunotherapy. However, limited knowledge regarding its mechanism of action and structure, or its binding partners with T cells, restrains the development of drug candidates that could unleash its full therapeutic potential. Here, we determine the crystal structure of Siglec-15 and delineate its binding epitope by co-crystallization with an anti-Siglec-15 blocking antibody. Saturation transfer-difference nuclear magnetic resonance (STD-NMR) spectroscopy assisted with molecular dynamics simulations reveals the binding mode of Siglec-15 to (2,3)- and 2,6)- linked sialic acids and to the cancer-associated sialyl-Tn (STn) glycoform. Binding of Siglec-15 to T cells, which lack STn expression, depends on the presence of (2,3)- and 2,6)- linked sialoglycans. We identify the leukocyte integrin CD11b as a binding partner of Siglec-15 on human T cells. Collectively, these data provide an integrative understanding of the structural features of Siglec-15 and underscore glycosylation as an additional layer of control of T cell responses.

2023-07-20 | PXD042009 | Pride

Proximity labeling of Siglec-1 counter-receptors on activated regulatory T cells using soluble Siglec-1-HRP multimers

Project description:Siglec-1 is a macrophage lectin-like receptor that mediates sialic acid-dependent cellular interactions. It was shown previously to promote inflammation in autoimmune disease through suppressing the expansion of regulatory T cells (Tregs). We have investigated the molecular basis for Siglec-1 binding to these cells using in vitro-induced Tregs. A proximity labelling and proteomics strategy were used to identify glycoproteins expressed by activated Tregs that may function as Siglec-1 counter-receptors.

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Proximity labeling of Siglec-1 counter-receptors on activated regulatory T cells using Siglec-1-HRP multimers on nano-beads

2021-04-28 | PXD021691 | Pride

Gene expression profiles of Siglec-14/THP-1 and Siglec-5/THP cell lines, with or without NTHi stimulation

Project description:Acquisition of a new strain of non-typeable Haemophilus influenzae (NTHi) is often associated with exacerbation of chronic obstructive pulmonary disease (COPD). We have previously reported that COPD patients who are homozygous null for SIGLEC14 gene is less susceptible to COPD exacerbation than those who have wild-type allele with functional SIGLEC14 gene. In order to gain insight into the mechanism behind the COPD exacerbation, and to find new clues that may lead to the discovery of objective biomarker of COPD exacerbation, Siglec-14/THP-1 and Siglec-5/THP-1 cell lines, which mimic monocytes from homozygous wild-type and homozygous SIGLEC14-null person, respectively, were incubated with or without NTHi, and their gene expression profiles were compared by using Affymetrix Human Genome U133 Plus 2.0 Array. Four samples (2 cell lines x 2 conditions) were analyzed. No replicates were made.

2014-08-04 | E-GEOD-47929 | biostudies-arrayexpress

Patient-derived anti-Siglec-6 antibodies engineered into T cell-recruiting bispecific antibody formats for treating leukemia

Project description:Despite numerous therapeutic options, safe and curative therapy is out of reach for most chronic lymphocytic leukemia (CLL) patients. We previously reported the identification of a patient-derived CLL-binding antibody, JML-1, and identified Siglec-6 as the target of JML-1. Siglec-6 is an attractive target for cancer immunotherapy due to its absence on healthy tissues and potential role in immune signaling. In this work, we identify additional patient-derived anti-Siglec-6 antibodies, RC-1 and RC-2, that bind with higher affinity than JML-1, yet exhibit similar specificity and overlapping conformational epitopes. Both JML-1 and RC-1 were employed to generate anti-Siglec-6 x anti-CD3 T cell-recruiting bispecific antibodies (T-biAbs) which were effective in vitro at activating T cells and lysing target cells. Upon engineering RC-1 into more compact and rigid T-biAb formats, we achieved sub-pM EC50 values for cell lysis in vitro. In addition, the T-biAbs mediated the killing of primary CLL cells by autologous T cells at natural effector-to-target cell ratios ex vivo. The increased potency of this T-biAb format appears to be due to the reduction in the length and/or flexibility of the cytolytic synapse. Furthermore, the anti-Siglec-6 x anti-CD3 T-biAb was effective at curing mice in a systemic in vivo model of CLL.

2022-12-19 | PXD029601 | Pride

The Inhibitory Receptor Siglec-8 Interacts with FcεRI and Globally Inhibits Intracellular Signaling in Primary Mast Cells Upon Activation

Project description:Immunomodulation of mast cell (MC) activity is warranted in allergic and inflammatory diseases where MCs have a central role in pathogenesis. Targeting Siglec-8, an inhibitory receptor on MCs and eosinophils, has shown promising activity in preclinical and clinical studies. While the intracellular pathways that regulate Siglec-8 activity in eosinophils have been well studied, the signaling mechanisms that lead to MC inhibition have not been fully elucidated. Here, we evaluate the intracellular signaling pathways of Siglec‐8‐mediated inhibition in primary MCs using an anti‐Siglec‐8 monoclonal antibody (mAb). Phospho‐proteomic profiling of FcεRI‐activated MCs revealed Siglec-8 mAb-treatment globally inhibited proximal and downstream kinases, leading to attenuated MC activation and degranulation. In fact, Siglec‐8 was found to directly interact with FcεRI signaling molecules. Siglec‐8 inhibition was dependent on both cytoplasmic immunoreceptor tyrosine-based inhibitory motifs (ITIMs) that interact with the SH2 containing protein phosphatase Shp-2 upon Siglec-8 phosphorylation. Taken together, these data support a model in which Siglec-8 regulates proximal FcεRI‐induced phosphorylation events through phosphatase recruitment and interaction with FcεRI, resulting in global inhibition of MCs upon Siglec-8 mAb engagement.

2022-01-21 | PXD030820 | Pride

Type-I interferon inducible genes 26 weeks after mCMV infection in Siglec-H wt and Siglec-H ko mice and their non infected controls

Project description:Type I interferons are critical anti-viral cytokines during virus infections and have also been implicated in the pathogenesis of systemic lupus erythematosus (SLE). The secretion of type I interferon of pDCs is modulated by Siglec-H, a DAP12 associated receptor on pDCs. We showed that Siglec-H deficient pDCs produce more of the type I interferon IFN-Î± in vitro and that Siglec-H ko mice produce more IFN-Î± after murine cytomegalovirus (mCMV) infection in vivo, leading to efficient clearance of the virus. Furthermore, ageing Siglec-H ko mice showed a mild form of systemic autoimmunity. In contrast, Siglec-H ko mice developed a severe form of systemic lupus-like autoimmune disease with strong kidney nephritis several weeks after a single mCMV infection. This induction of systemic autoimmune disease after virus infection in Siglec-H ko mice was accompanied by a type I interferon signature and fully dependent on type I interferon signaling. These results show that Siglec-H normally serves as modulator of type I interferon responses after infection with a persistent virus and thereby prevents induction of autoimmune disease. For microarray experiments gene expression profiles of total splenic cells from two wt and Siglec-H ko mice 26 weeks after infection with luciferase expressing murine Cytomegalovirus (5x105 pfu) or from two uninfected wt and Siglec-H ko control mice were analyzed

2016-03-16 | E-GEOD-79248 | biostudies-arrayexpress

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