Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
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Heparan sulfates from bat and human lung and their binding to the spike protein of SARS-CoV-2 virus, L. Yan, Y. Song, K. Xia, P. He, F. Zhang, S. Chen, Ro. Pouliot, D. J. Weiss, R. Tandon, J. T. Bates, D. R. Ederer, D. Mitra, P. Sharma, A. Davis, R. J. Linhardt, Carbohydrate Polymers, 260, 117797, 2021.
Severe acute respiratory syndrome-related coronavirus-2 (SARS-CoV-2) has resulted in a pandemic and continues to spread at an unprecedented rate around the world. Although a vaccine has recently been approved, there are currently few effective therapeutics to fight its associated disease in humans, COVID-19. SARS-CoV-2 and the related severe acute respiratory syndrome (SARS-CoV-1), and Middle East respiratory syndrome (MERS-CoV) result from zoonotic respiratory viruses that have bats as the primary host and an as yet unknown secondary host. While each of these viruses has different protein-based cell-surface receptors, each rely on the glycosaminoglycan, heparan sulfate as a co-receptor. In this study we compare, for the first time, differences and similarities in the structure of heparan sulfate in human and bat lungs. Furthermore, we show that the spike glycoprotein of COVID-19 binds 3.5 times stronger to human lung heparan sulfate than bat lung heparan sulfate.;
Carbohydrate Polymers, 260, 117797; Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
The Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; Carbohydrate Polymers; https://harc.rpi.edu/;