PMC:7128678 / 21337-22204 JSONTXT

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{"project":"LitCovid-sentences","denotations":[{"id":"T180","span":{"begin":110,"end":226},"obj":"Sentence"},{"id":"T181","span":{"begin":227,"end":376},"obj":"Sentence"},{"id":"T182","span":{"begin":377,"end":610},"obj":"Sentence"},{"id":"T183","span":{"begin":611,"end":867},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Dual recognition of gangliosides and angiotensin-converting enzyme-2 (ACE-2) by SARS-CoV-2 spike (S) protein. The viral protein displays two distinct domains, the tips of which are available for distinct types of interactions. The receptor-binding domain binds to the ACE-2 receptor, and the N-terminal domain (NTD) binds to the ganglioside-rich domain of the plasma membrane. Lipid rafts, which are membrane domains enriched in gangliosides (in yellow) and cholesterol (in blue), provide a perfect attractive interface for adequately positioning the viral S protein at the first step of the infection process. These structural and molecular modelling studies suggest that amino acid residues 111–162 of the NTD form a functional ganglioside-binding domain, the interaction of which with lipid rafts can be efficiently prevented by chloroquine and hydroxychloroquine."}