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7CN9

Cryo-EM structure of SARS-CoV-2 Spike ectodomain

Summary for 7CN9
Entry DOI10.2210/pdb7cn9/pdb
EMDB information30419
DescriptorSpike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
Functional Keywordssars-cov-2, spike, fully glycosylated, viral protein
Biological sourceSevere acute respiratory syndrome coronavirus 2 (2019-nCoV)
Total number of polymer chains3
Total formula weight385298.72
Authors
Ho, M.,Chang, Y.,Wang, C.,Wu, Y.,Huang, H.,Chen, T.,Lo, J.M.,Chen, X.,Ma, C. (deposition date: 2020-07-30, release date: 2020-08-26, Last modification date: 2024-11-06)
Primary citationLiu, Y.M.,Shahed-Al-Mahmud, M.,Chen, X.,Chen, T.H.,Liao, K.S.,Lo, J.M.,Wu, Y.M.,Ho, M.C.,Wu, C.Y.,Wong, C.H.,Jan, J.T.,Ma, C.
A Carbohydrate-Binding Protein from the Edible Lablab Beans Effectively Blocks the Infections of Influenza Viruses and SARS-CoV-2.
Cell Rep, 32:108016-108016, 2020
Cited by
PubMed Abstract: The 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.
PubMed: 32755598
DOI: 10.1016/j.celrep.2020.108016
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.7 Å)
Structure validation

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