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Cryo-EM structure of SARS-CoV-2 Spike ectodomainCryo-EM structure of SARS-CoV-2 Spike ectodomain
Structural highlights
Publication Abstract from PubMedThe influenza virus hemagglutinin (HA) and coronavirus spike (S) protein mediate virus entry. HA and S proteins are heavily glycosylated, making them potential targets for carbohydrate binding agents such as lectins. Here, we show that the lectin FRIL, isolated from hyacinth beans (Lablab purpureus), has anti-influenza and anti-SARS-CoV-2 activity. FRIL can neutralize 11 representative human and avian influenza strains at low nanomolar concentrations, and intranasal administration of FRIL is protective against lethal H1N1 infection in mice. FRIL binds preferentially to complex-type N-glycans and neutralizes viruses that possess complex-type N-glycans on their envelopes. As a homotetramer, FRIL is capable of aggregating influenza particles through multivalent binding and trapping influenza virions in cytoplasmic late endosomes, preventing their nuclear entry. Remarkably, FRIL also effectively neutralizes SARS-CoV-2, preventing viral protein production and cytopathic effect in host cells. These findings suggest a potential application of FRIL for the prevention and/or treatment of influenza and COVID-19. A Carbohydrate-Binding Protein from the Edible Lablab Beans Effectively Blocks the Infections of Influenza Viruses and SARS-CoV-2.,Liu YM, Shahed-Al-Mahmud M, Chen X, Chen TH, Liao KS, Lo JM, Wu YM, Ho MC, Wu CY, Wong CH, Jan JT, Ma C Cell Rep. 2020 Aug 11;32(6):108016. doi: 10.1016/j.celrep.2020.108016. Epub 2020 , Jul 24. PMID:32755598[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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