SARS-CoV-2 and other coronaviruses bind to phosphorylated glycans from the human lung

• Type of Material: Article
• Authors: Lauren Byrd-Leotis, Emory University; Yi Lasanajak, Emory University; Thomas Bowen, Emory University; Kelly Baker, Emory University; Xuezheng Song, Emory University; Mehul Suthar, Emory University; Richard Cummings, Emory University; David Steinhauer, Emory University
• Language: English
• Date: 2021-10-01
• Publisher: Elsevier
• Publication Version: Final Published Version
• Copyright Statement: © 2021 Elsevier Inc.
• Final Published Version (URL): http://dx.doi.org/10.1016/j.virol.2021.07.012
• Title of Journal or Parent Work: VIROLOGY
• Volume: 562
• Start Page: 142
• End Page: 148
• Grant/Funding Information: The authors acknowledge support by the U.S. Department of Health and Human Services contract HHSN272201400004C (NIAID Centers of Excellence for Influenza Research and Surveillance) and the National Institutes of Health award P41GM103694 and R24GM137763 to RDC and the National Center for Functional Glycomics, which supports the use of the Consortium for Functional Glycomics glycan microarrays. This study was assisted in part by the Emory Glycomics and Molecular Interactions Core (EGMIC), which is subsidized by the Emory University School of Medicine and is one of the Emory Integrated Core Facilities.
• Keywords: Phosphorylated glycans; Coronavirus receptors; SARS-CoV-2; Glycan receptors; Human lung glycan microarray
• Research Categories: Biology, Virology; Health Sciences, Public Health

Abstract

SARS-CoV, MERS-CoV, and potentially SARS-CoV-2 emerged as novel human coronaviruses following cross-species transmission from animal hosts. Although the receptor binding characteristics of human coronaviruses are well documented, the role of carbohydrate binding in addition to recognition of proteinaceous receptors has not been fully explored. Using natural glycan microarray technology, we identified N-glycans in the human lung that are recognized by various human and animal coronaviruses. All viruses tested, including SARS-CoV-2, bound strongly to a range of phosphorylated, high mannose N-glycans and to a very specific set of sialylated structures. Examination of two linked strains, human CoV OC43 and bovine CoV Mebus, reveals shared binding to the sialic acid form Neu5Gc (not found in humans), supporting the evidence for cross-species transmission of the bovine strain. Our findings, revealing robust recognition of lung glycans, suggest that these receptors could play a role in the initial stages of coronavirus attachment and entry.