PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 33106801-6 2020 The spike and ACE2 proteins are highly glycosylated with sialic acid modifications that direct viral-host interactions and infection. N-Acetylneuraminic Acid 57-68 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 4-9 33264497-3 2021 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 76-87 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 23-28 33264497-3 2021 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 76-87 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 30-31 33264497-3 2021 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 215-226 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 23-28 33264497-3 2021 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 215-226 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 30-31 34013301-2 2021 Cross-reactive antibodies specifically recognized the sialic acid moiety on N-linked glycans of the Spike protein and do not neutralize in vitro SARS-CoV-2. N-Acetylneuraminic Acid 54-65 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 100-105 33909065-5 2021 In particular, a flat sialic acid-binding domain was proposed at the N-terminal domain (NTD) of the spike protein, which may lead to the initial contact and interaction of the virus on the epithelium followed by higher affinity binding to ACE2 receptor, likely a two-step attachment fashion. N-Acetylneuraminic Acid 22-33 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 100-105 33254482-7 2020 Based on this survey, we hypothesize that the correlation between the ABO blood system and susceptibility to SARS-CoV-2 infection can be presumably explained by the modulation of sialic acid-containing receptors distribution on host cell surface induced by ABO antigens through carbohydrate-carbohydrate interactions, which could maximize or minimize the virus Spike protein binding to the host cell. N-Acetylneuraminic Acid 179-190 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 361-366 34634204-3 2021 Herein, we develop a prototype flow-through device (related, but distinct to LFDs), utilizing N-acetyl neuraminic acid-functionalized, polymer-coated, gold nanoparticles as the detection/capture unit for SARS-COV-2, by targeting the sialic acid-binding site of the spike protein. N-Acetylneuraminic Acid 94-118 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 265-270 33823179-6 2021 The spike and ACE2 proteins are highly glycosylated with sialic acid modifications that direct viral-host interactions and infection. N-Acetylneuraminic Acid 57-68 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 4-9 33082935-6 2020 Finally, a key domain in the spike protein of SARS-CoV2 has been shown to bind N-acetylneuraminic acid (Neu5Ac), a process that may be essential to cell entry by the virus. N-Acetylneuraminic Acid 79-102 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 29-34 33082935-6 2020 Finally, a key domain in the spike protein of SARS-CoV2 has been shown to bind N-acetylneuraminic acid (Neu5Ac), a process that may be essential to cell entry by the virus. N-Acetylneuraminic Acid 104-110 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 29-34 34754101-2 2022 Here, we reveal that the receptor-binding domain (RBD) of the spike (S) protein on SARS-CoV-2 recognizes oligosaccharides containing sialic acid (Sia), with preference for monosialylated gangliosides. N-Acetylneuraminic Acid 133-144 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 62-67 34754101-2 2022 Here, we reveal that the receptor-binding domain (RBD) of the spike (S) protein on SARS-CoV-2 recognizes oligosaccharides containing sialic acid (Sia), with preference for monosialylated gangliosides. N-Acetylneuraminic Acid 133-144 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 69-70 34754101-2 2022 Here, we reveal that the receptor-binding domain (RBD) of the spike (S) protein on SARS-CoV-2 recognizes oligosaccharides containing sialic acid (Sia), with preference for monosialylated gangliosides. N-Acetylneuraminic Acid 146-149 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 62-67 34754101-2 2022 Here, we reveal that the receptor-binding domain (RBD) of the spike (S) protein on SARS-CoV-2 recognizes oligosaccharides containing sialic acid (Sia), with preference for monosialylated gangliosides. N-Acetylneuraminic Acid 146-149 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 69-70 34634204-3 2021 Herein, we develop a prototype flow-through device (related, but distinct to LFDs), utilizing N-acetyl neuraminic acid-functionalized, polymer-coated, gold nanoparticles as the detection/capture unit for SARS-COV-2, by targeting the sialic acid-binding site of the spike protein. N-Acetylneuraminic Acid 233-244 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 265-270 34631661-0 2021 A Linkage-specific Sialic Acid Labeling Strategy Reveals Different Site-specific Glycosylation Patterns in SARS-CoV-2 Spike Protein Produced in CHO and HEK Cell Substrates. N-Acetylneuraminic Acid 19-30 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 118-123 35273357-4 2022 Sialic acid on the host cell surface is the key molecule to which histones bridge subunit 2 of the S protein. N-Acetylneuraminic Acid 0-11 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 99-100 34368076-7 2021 To address this question, we took N-Acetylneuraminic acid (Neu5Ac), a type of predominant sialic acid found in human cells, as the molecular probe to computationally search the surface of the spike protein to locate the potential binding sites of Neu5Ac. N-Acetylneuraminic Acid 34-57 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 192-197 34368076-7 2021 To address this question, we took N-Acetylneuraminic acid (Neu5Ac), a type of predominant sialic acid found in human cells, as the molecular probe to computationally search the surface of the spike protein to locate the potential binding sites of Neu5Ac. N-Acetylneuraminic Acid 59-65 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 192-197 34368076-7 2021 To address this question, we took N-Acetylneuraminic acid (Neu5Ac), a type of predominant sialic acid found in human cells, as the molecular probe to computationally search the surface of the spike protein to locate the potential binding sites of Neu5Ac. N-Acetylneuraminic Acid 90-101 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 192-197 34368076-7 2021 To address this question, we took N-Acetylneuraminic acid (Neu5Ac), a type of predominant sialic acid found in human cells, as the molecular probe to computationally search the surface of the spike protein to locate the potential binding sites of Neu5Ac. N-Acetylneuraminic Acid 247-253 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 192-197 34179095-4 2021 Our results indicate that SARS-CoV-2 uses a dual strategy: in addition to the known interaction with angiotensin-converting enzyme 2, the viral spike protein can also interact with sialic-acid receptors of the cells in the upper airways. N-Acetylneuraminic Acid 181-192 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 144-149 35191576-1 2022 The interaction of the SARS CoV2 spike glycoprotein with two sialic acid-containing trisaccharides (a2,3 and a2,6 sialyl N-Acetyllactosamine) has been demonstrated by NMR. N-Acetylneuraminic Acid 61-72 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 33-38 35191576-2 2022 The NMR-based distinction between the signals of those sialic acids in the glycans covalently attached to the spike protein and those belonging to the exogenous a2,3 and a2,6 sialyl N-Acetyllactosamine ligands has been achieved by synthesizing uniformly 13C-labelled trisaccharides at the sialic acid and galactose moieties. N-Acetylneuraminic Acid 289-300 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 110-115 35191576-4 2022 Additional experiments with the spike protein in the presence of a specific antibody for the N-terminal domain and with the isolated receptor binding and N-terminal domains of the spike protein unambiguously show that the sialic acid binding site is located at the N-terminal domain. N-Acetylneuraminic Acid 222-233 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 32-37 35191576-4 2022 Additional experiments with the spike protein in the presence of a specific antibody for the N-terminal domain and with the isolated receptor binding and N-terminal domains of the spike protein unambiguously show that the sialic acid binding site is located at the N-terminal domain. N-Acetylneuraminic Acid 222-233 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 180-185