Unveiling Molecular Recognition of Sialoglycans by Human Siglec-10
Summary: Siglec-10 is an inhibitory I-type lectin selectively recognizing sialoglycans exposed on cell surfaces, involved in several patho-physiological processes. The key role Siglec-10 plays in the regulation of immune cell functions has made it a potential target for the development of immunother...
| Main Authors: | , , , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2020-06-01
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| Series: | iScience |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2589004220304168 |
| _version_ | 1818176784318857216 |
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| author | Rosa Ester Forgione Cristina Di Carluccio Juan Guzmán-Caldentey Rosa Gaglione Filomena Battista Fabrizio Chiodo Yoshiyuki Manabe Angela Arciello Pompea Del Vecchio Koichi Fukase Antonio Molinaro Sonsoles Martín-Santamaría Paul R. Crocker Roberta Marchetti Alba Silipo |
| author_facet | Rosa Ester Forgione Cristina Di Carluccio Juan Guzmán-Caldentey Rosa Gaglione Filomena Battista Fabrizio Chiodo Yoshiyuki Manabe Angela Arciello Pompea Del Vecchio Koichi Fukase Antonio Molinaro Sonsoles Martín-Santamaría Paul R. Crocker Roberta Marchetti Alba Silipo |
| author_sort | Rosa Ester Forgione |
| collection | DOAJ |
| description | Summary: Siglec-10 is an inhibitory I-type lectin selectively recognizing sialoglycans exposed on cell surfaces, involved in several patho-physiological processes. The key role Siglec-10 plays in the regulation of immune cell functions has made it a potential target for the development of immunotherapeutics against a broad range of diseases. However, the crystal structure of the protein has not been resolved for the time being and the atomic description of Siglec-10 interactions with complex glycans has not been previously unraveled. We present here the first insights of the molecular mechanisms regulating the interaction between Siglec-10 and naturally occurring sialoglycans. We used combined spectroscopic, computational and biophysical approaches to dissect glycans' epitope mapping and conformation upon binding in order to afford a description of the 3D complexes. Our outcomes provide a structural perspective for the rational design and development of high-affinity ligands to control the receptor functionality. |
| first_indexed | 2024-12-11T20:21:41Z |
| format | Article |
| id | doaj.art-2f7d7acbcd0a4054aa318c59eb945639 |
| institution | Directory Open Access Journal |
| issn | 2589-0042 |
| language | English |
| last_indexed | 2024-12-11T20:21:41Z |
| publishDate | 2020-06-01 |
| publisher | Elsevier |
| record_format | Article |
| series | iScience |
| spelling | doaj.art-2f7d7acbcd0a4054aa318c59eb9456392022-12-22T00:52:04ZengElsevieriScience2589-00422020-06-01236101231Unveiling Molecular Recognition of Sialoglycans by Human Siglec-10Rosa Ester Forgione0Cristina Di Carluccio1Juan Guzmán-Caldentey2Rosa Gaglione3Filomena Battista4Fabrizio Chiodo5Yoshiyuki Manabe6Angela Arciello7Pompea Del Vecchio8Koichi Fukase9Antonio Molinaro10Sonsoles Martín-Santamaría11Paul R. Crocker12Roberta Marchetti13Alba Silipo14Dipartimento di Scienze Chimiche, Complesso Universitario Monte Sant’Angelo, Università di Napoli Federico II, Via Cintia 4, 80126 Napoli, ItalyDipartimento di Scienze Chimiche, Complesso Universitario Monte Sant’Angelo, Università di Napoli Federico II, Via Cintia 4, 80126 Napoli, ItalyDepartment of Structural & Chemical Biology, Centro de Investigaciones Biológicas ''Margarita Salas'', CIB-CSIC, C/ Ramiro de Maeztu 9, 28040 Madrid, SpainDipartimento di Scienze Chimiche, Complesso Universitario Monte Sant’Angelo, Università di Napoli Federico II, Via Cintia 4, 80126 Napoli, ItalyDipartimento di Scienze Chimiche, Complesso Universitario Monte Sant’Angelo, Università di Napoli Federico II, Via Cintia 4, 80126 Napoli, ItalyAmsterdam UMC, Vrije Universiteit Amsterdam, Department of Molecular Cell Biology and Immunology, Amsterdam Infection and Immunity Institute, Amsterdam, the NetherlandsDepartment of Chemistry, Graduate School of Science, Osaka University, Osaka, JapanDipartimento di Scienze Chimiche, Complesso Universitario Monte Sant’Angelo, Università di Napoli Federico II, Via Cintia 4, 80126 Napoli, ItalyDipartimento di Scienze Chimiche, Complesso Universitario Monte Sant’Angelo, Università di Napoli Federico II, Via Cintia 4, 80126 Napoli, ItalyDepartment of Chemistry, Graduate School of Science, Osaka University, Osaka, JapanDipartimento di Scienze Chimiche, Complesso Universitario Monte Sant’Angelo, Università di Napoli Federico II, Via Cintia 4, 80126 Napoli, Italy; Department of Chemistry, Graduate School of Science, Osaka University, Osaka, JapanDepartment of Structural & Chemical Biology, Centro de Investigaciones Biológicas ''Margarita Salas'', CIB-CSIC, C/ Ramiro de Maeztu 9, 28040 Madrid, SpainDivision of Cell Signalling and Immunology, School of Life Sciences, University of Dundee, Dundee, UKDipartimento di Scienze Chimiche, Complesso Universitario Monte Sant’Angelo, Università di Napoli Federico II, Via Cintia 4, 80126 Napoli, Italy; Corresponding authorDipartimento di Scienze Chimiche, Complesso Universitario Monte Sant’Angelo, Università di Napoli Federico II, Via Cintia 4, 80126 Napoli, Italy; Corresponding authorSummary: Siglec-10 is an inhibitory I-type lectin selectively recognizing sialoglycans exposed on cell surfaces, involved in several patho-physiological processes. The key role Siglec-10 plays in the regulation of immune cell functions has made it a potential target for the development of immunotherapeutics against a broad range of diseases. However, the crystal structure of the protein has not been resolved for the time being and the atomic description of Siglec-10 interactions with complex glycans has not been previously unraveled. We present here the first insights of the molecular mechanisms regulating the interaction between Siglec-10 and naturally occurring sialoglycans. We used combined spectroscopic, computational and biophysical approaches to dissect glycans' epitope mapping and conformation upon binding in order to afford a description of the 3D complexes. Our outcomes provide a structural perspective for the rational design and development of high-affinity ligands to control the receptor functionality.http://www.sciencedirect.com/science/article/pii/S2589004220304168BiochemistryBiochemistry MethodsStructural BiologyData Analysis in Structural Biology |
| spellingShingle | Rosa Ester Forgione Cristina Di Carluccio Juan Guzmán-Caldentey Rosa Gaglione Filomena Battista Fabrizio Chiodo Yoshiyuki Manabe Angela Arciello Pompea Del Vecchio Koichi Fukase Antonio Molinaro Sonsoles Martín-Santamaría Paul R. Crocker Roberta Marchetti Alba Silipo Unveiling Molecular Recognition of Sialoglycans by Human Siglec-10 iScience Biochemistry Biochemistry Methods Structural Biology Data Analysis in Structural Biology |
| title | Unveiling Molecular Recognition of Sialoglycans by Human Siglec-10 |
| title_full | Unveiling Molecular Recognition of Sialoglycans by Human Siglec-10 |
| title_fullStr | Unveiling Molecular Recognition of Sialoglycans by Human Siglec-10 |
| title_full_unstemmed | Unveiling Molecular Recognition of Sialoglycans by Human Siglec-10 |
| title_short | Unveiling Molecular Recognition of Sialoglycans by Human Siglec-10 |
| title_sort | unveiling molecular recognition of sialoglycans by human siglec 10 |
| topic | Biochemistry Biochemistry Methods Structural Biology Data Analysis in Structural Biology |
| url | http://www.sciencedirect.com/science/article/pii/S2589004220304168 |
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