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TitleA Carbohydrate-Binding Protein from the Edible Lablab Beans Effectively Blocks the Infections of Influenza Viruses and SARS-CoV-2.
Journal, issue, pagesCell Rep, Vol. 32, Issue 6, Page 108016, Year 2020
Publish dateAug 11, 2020
AuthorsYo-Min Liu / Md Shahed-Al-Mahmud / Xiaorui Chen / Ting-Hua Chen / Kuo-Shiang Liao / Jennifer M Lo / Yi-Min Wu / Meng-Chiao Ho / Chung-Yi Wu / Chi-Huey Wong / Jia-Tsrong Jan / Che Ma /
PubMed AbstractThe 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 ...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.
External linksCell Rep / PubMed:32755598 / PubMed Central
MethodsEM (single particle)
Resolution4.7 - 27.59 Å
Structure data

EMDB-30380:
Negative stain density of the tetrameric FRIL in solution
Method: EM (single particle) / Resolution: 27.59 Å

EMDB-30381:
Cryo-EM density of SARS-CoV-2 spike protein
Method: EM (single particle) / Resolution: 4.7 Å

EMDB-30419, PDB-7cn9:
Cryo-EM structure of SARS-CoV-2 Spike ectodomain
Method: EM (single particle) / Resolution: 4.7 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

Source
  • Lablab purpureus (antaque)
  • severe acute respiratory syndrome coronavirus 2
KeywordsVIRAL PROTEIN / SARS-CoV-2 / spike / fully glycosylated

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