Title : The structural basis of accelerated host cell entry by SARS-CoV-2†.

Pub. Date : 2021 Sep

PMID : 33264497






4 Functional Relationships(s)
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Protein Name
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1 Based on notable viral spike (S) protein features, we propose that the flat sialic acid-binding domain at the N-terminal domain (NTD) of the S1 subunit leads to more effective first contact and interaction with the sialic acid layer over the epithelium and this, in turn, allows faster viral "surfing" of the epithelium and receptor scanning by SARS-CoV-2. N-Acetylneuraminic Acid surface glycoprotein Severe acute respiratory syndrome coronavirus 2
2 Based on notable viral spike (S) protein features, we propose that the flat sialic acid-binding domain at the N-terminal domain (NTD) of the S1 subunit leads to more effective first contact and interaction with the sialic acid layer over the epithelium and this, in turn, allows faster viral "surfing" of the epithelium and receptor scanning by SARS-CoV-2. N-Acetylneuraminic Acid surface glycoprotein Severe acute respiratory syndrome coronavirus 2
3 Based on notable viral spike (S) protein features, we propose that the flat sialic acid-binding domain at the N-terminal domain (NTD) of the S1 subunit leads to more effective first contact and interaction with the sialic acid layer over the epithelium and this, in turn, allows faster viral "surfing" of the epithelium and receptor scanning by SARS-CoV-2. N-Acetylneuraminic Acid surface glycoprotein Severe acute respiratory syndrome coronavirus 2
4 Based on notable viral spike (S) protein features, we propose that the flat sialic acid-binding domain at the N-terminal domain (NTD) of the S1 subunit leads to more effective first contact and interaction with the sialic acid layer over the epithelium and this, in turn, allows faster viral "surfing" of the epithelium and receptor scanning by SARS-CoV-2. N-Acetylneuraminic Acid surface glycoprotein Severe acute respiratory syndrome coronavirus 2