Identification of Siglec Ligands Using a Proximity Labeling Method
Siglecs are a family of receptor-type glycan recognition proteins (lectins) involved in self–nonself discrimination by the immune system. Identification of Siglec ligands is necessary to understand how Siglec–ligand interaction translates into biological outcomes. However, this is challenging becaus...
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Published in | Journal of proteome research Vol. 16; no. 10; pp. 3929 - 3941 |
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Main Authors | , , , , , , , , , |
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American Chemical Society
06.10.2017
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Abstract | Siglecs are a family of receptor-type glycan recognition proteins (lectins) involved in self–nonself discrimination by the immune system. Identification of Siglec ligands is necessary to understand how Siglec–ligand interaction translates into biological outcomes. However, this is challenging because the interaction is weak. To facilitate identification of Siglec ligands, we adopted a proximity labeling method based on the tyramide radicalization principle. Cells that express Siglec ligands were labeled with Siglec–peroxidase complexes and incubated with biotin tyramide and hydrogen peroxide to generate short-lived tyramide radicals that covalently label the proteins near the Siglec–peroxidase complex. A proof-of-principle experiment using CD22 (Siglec-2) probe identified its known ligands on B cells, including CD22 itself, CD45, and IgM, among others, demonstrating the validity of this method. The specificity of labeling was confirmed by sialidase treatment of target cells and using glycan recognition-deficient mutant CD22 probes. Moreover, possible interactions between biotin-labeled proteins were revealed by literature-based protein–protein interaction network analysis, implying the presence of a molecular cluster comprising CD22 ligands. Further application of this method identified CD44 as a hitherto unknown Siglec-15 ligand on RAW264.7-derived osteoclasts. These results demonstrated the utility of proximity labeling for the identification of Siglec ligands, which may extend to other lectins. |
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AbstractList | Siglecs are a family of receptor-type glycan recognition proteins (lectins) involved in self-nonself discrimination by the immune system. Identification of Siglec ligands is necessary to understand how Siglec-ligand interaction translates into biological outcomes. However, this is challenging because the interaction is weak. To facilitate identification of Siglec ligands, we adopted a proximity labeling method based on the tyramide radicalization principle. Cells that express Siglec ligands were labeled with Siglec-peroxidase complexes and incubated with biotin tyramide and hydrogen peroxide to generate short-lived tyramide radicals that covalently label the proteins near the Siglec-peroxidase complex. A proof-of-principle experiment using CD22 (Siglec-2) probe identified its known ligands on B cells, including CD22 itself, CD45, and IgM, among others, demonstrating the validity of this method. The specificity of labeling was confirmed by sialidase treatment of target cells and using glycan recognition-deficient mutant CD22 probes. Moreover, possible interactions between biotin-labeled proteins were revealed by literature-based protein-protein interaction network analysis, implying the presence of a molecular cluster comprising CD22 ligands. Further application of this method identified CD44 as a hitherto unknown Siglec-15 ligand on RAW264.7-derived osteoclasts. These results demonstrated the utility of proximity labeling for the identification of Siglec ligands, which may extend to other lectins. |
Author | Low, Penk-Yeir Lin, Chun-Cheng Chen, Yu-Ju Chen, Yi-Ju Ventura, Albert Angata, Takashi Chang, Lanyi Chen, Yi-Hsiu Fan, Chan-Yo Tang, Chin-Ju |
AuthorAffiliation | Department of Chemistry Institute of Biological Chemistry Institute of Chemistry National Taiwan University Institute of Biochemical Sciences |
AuthorAffiliation_xml | – name: Institute of Biological Chemistry – name: – name: Institute of Chemistry – name: Department of Chemistry – name: National Taiwan University – name: Institute of Biochemical Sciences |
Author_xml | – sequence: 1 givenname: Lanyi surname: Chang fullname: Chang, Lanyi – sequence: 2 givenname: Yi-Ju surname: Chen fullname: Chen, Yi-Ju – sequence: 3 givenname: Chan-Yo surname: Fan fullname: Fan, Chan-Yo organization: Department of Chemistry – sequence: 4 givenname: Chin-Ju surname: Tang fullname: Tang, Chin-Ju – sequence: 5 givenname: Yi-Hsiu surname: Chen fullname: Chen, Yi-Hsiu – sequence: 6 givenname: Penk-Yeir surname: Low fullname: Low, Penk-Yeir – sequence: 7 givenname: Albert surname: Ventura fullname: Ventura, Albert – sequence: 8 givenname: Chun-Cheng surname: Lin fullname: Lin, Chun-Cheng organization: Department of Chemistry – sequence: 9 givenname: Yu-Ju orcidid: 0000-0002-3178-6697 surname: Chen fullname: Chen, Yu-Ju – sequence: 10 givenname: Takashi orcidid: 0000-0002-4171-702X surname: Angata fullname: Angata, Takashi email: angata@gate.sinica.edu.tw organization: National Taiwan University |
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Snippet | Siglecs are a family of receptor-type glycan recognition proteins (lectins) involved in self–nonself discrimination by the immune system. Identification of... Siglecs are a family of receptor-type glycan recognition proteins (lectins) involved in self-nonself discrimination by the immune system. Identification of... |
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SubjectTerms | Animals B-Lymphocytes - immunology Biotin - chemistry Free Radicals - chemistry Humans Hydrogen Peroxide - chemistry Immune System - chemistry Immune System - immunology Immunoglobulin M - immunology Lectins - immunology Lectins - metabolism Leukocyte Common Antigens - immunology Ligands Mice RAW 264.7 Cells Sialic Acid Binding Ig-like Lectin 2 - chemistry Sialic Acid Binding Ig-like Lectin 2 - immunology Sialic Acid Binding Immunoglobulin-like Lectins - immunology Sialic Acid Binding Immunoglobulin-like Lectins - metabolism Staining and Labeling Tyramine - chemistry |
Title | Identification of Siglec Ligands Using a Proximity Labeling Method |
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