Pathogen-sugar interactions revealed by universal saturation transfer analysis-Reference-Cited by-同舟云学术

Pathogen-sugar interactions revealed by universal saturation transfer analysis

Published:2022-07-22 Issue:6604 Volume:377 Page:
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Buchanan Charles J.¹²³^ORCID,Gaunt Ben¹^ORCID,Harrison Peter J.⁴⁵^ORCID,Yang Yun¹⁴^ORCID,Liu Jiwei¹,Khan Aziz¹²^ORCID,Giltrap Andrew M.¹²^ORCID,Le Bas Audrey¹⁴^ORCID,Ward Philip N.⁴^ORCID,Gupta Kapil⁶^ORCID,Dumoux Maud¹^ORCID,Tan Tiong Kit⁷^ORCID,Schimaski Lisa⁷,Daga Sergio⁸⁹^ORCID,Picchiotti Nicola¹⁰¹¹^ORCID,Baldassarri Margherita⁸⁹^ORCID,Benetti Elisa⁹^ORCID,Fallerini Chiara⁸⁹^ORCID,Fava Francesca⁸⁹¹²^ORCID,Giliberti Annarita⁸⁹,Koukos Panagiotis I.¹³,Davy Matthew J.¹^ORCID,Lakshminarayanan Abirami¹²^ORCID,Xue Xiaochao²¹⁴^ORCID,Papadakis Georgios²,Deimel Lachlan P.¹⁴^ORCID,Casablancas-Antràs Virgínia²³^ORCID,Claridge Timothy D. W.²^ORCID,Bonvin Alexandre M. J. J.¹³^ORCID,Sattentau Quentin J.¹⁴^ORCID,Furini Simone⁹^ORCID,Gori Marco¹⁰¹⁵,Huo Jiandong¹⁴^ORCID,Owens Raymond J.¹⁴^ORCID,Schaffitzel Christiane¹³^ORCID,Berger Imre¹³^ORCID,Renieri Alessandra⁸⁹¹²^ORCID,Naismith James H.¹⁴^ORCID,Baldwin Andrew J.¹²³^ORCID,Davis Benjamin G.¹²¹⁶^ORCID,

Affiliation:

1. Rosalind Franklin Institute, Harwell Science and Innovation Campus, Oxford OX11 0FA, UK.

2. Department of Chemistry, University of Oxford, Oxford OX1 3TA, UK.

3. Kavli Institute of Nanoscience Discovery, University of Oxford, Oxford OX1 3QU, UK.

4. Division of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Headington, Oxford OX3 7BN, UK.

5. Diamond Light Source, Harwell Science and Innovation Campus, Oxfordshire, UK.

6. Max Planck Bristol Centre for Minimal Biology, University of Bristol, Bristol, UK.

7. MRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Oxford, UK.

8. Medical Genetics, University of Siena, Siena, Italy.

9. Med Biotech Hub and Competence Center, Department of Medical Biotechnologies, University of Siena, Siena, Italy.

10. Department of Information Engineering and Mathematics, University of Siena, Siena, Italy.

11. Department of Mathematics, University of Pavia, Pavia, Italy.

12. Genetica Medica, Azienda Ospedaliera Universitaria Senese, Siena, Italy.

13. Bijvoet Centre for Biomolecular Research, Faculty of Science, Utrecht University, Utrecht, Netherlands.

14. Sir William Dunn School of Pathology, Oxford, UK.

15. Maasai, I3S CNRS, Université Côte d’Azur, Nice, France.

16. Department of Pharmacology, University of Oxford, Oxford OX1 3QT, UK.

Abstract

Many pathogens exploit host cell-surface glycans. However, precise analyses of glycan ligands binding with heavily modified pathogen proteins can be confounded by overlapping sugar signals and/or compounded with known experimental constraints. Universal saturation transfer analysis (uSTA) builds on existing nuclear magnetic resonance spectroscopy to provide an automated workflow for quantitating protein-ligand interactions. uSTA reveals that early-pandemic, B-origin-lineage severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike trimer binds sialoside sugars in an “end-on” manner. uSTA-guided modeling and a high-resolution cryo–electron microscopy structure implicate the spike N-terminal domain (NTD) and confirm end-on binding. This finding rationalizes the effect of NTD mutations that abolish sugar binding in SARS-CoV-2 variants of concern. Together with genetic variance analyses in early pandemic patient cohorts, this binding implicates a sialylated polylactosamine motif found on tetraantennary N-linked glycoproteins deep in the human lung as potentially relevant to virulence and/or zoonosis.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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