PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 34015061-4 2021 DC-SIGN, L-SIGN, Langerin and MGL bind to diverse glycans of the spike using multiple interaction areas. Polysaccharides 50-57 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 65-70 34004174-4 2021 Comparison of the glycosylation profile of the S protein to that of the HLA-II-bound S peptides reveals substantial trimming of glycan residues on the latter, likely induced during antigen processing. Polysaccharides 128-134 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 47-48 34004174-4 2021 Comparison of the glycosylation profile of the S protein to that of the HLA-II-bound S peptides reveals substantial trimming of glycan residues on the latter, likely induced during antigen processing. Polysaccharides 128-134 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 85-86 33991349-2 2021 Spike glycan processing and cleavage, which occur in the Golgi network, are important for fusion at the plasma membrane, promoting both virion infectivity and cell-to-cell viral spreading. Polysaccharides 6-12 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 0-5 34013265-8 2021 A local analysis of seven key binding pockets reveals that six out them, including those for engaging ACE2, therapeutic mini-proteins, linoleic acid, two different kinds of antibodies, and protein-glycan interaction sites, switch conformations between their known apo- and holo-conformations, even when the global spike conformation is 1RBD-up. Polysaccharides 197-203 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 314-319 33903171-5 2021 Interestingly, the glycans at two glycosylation sites, N90 and N322, have opposite effects on spike protein binding. Polysaccharides 19-26 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 94-99 34013268-5 2021 Comparison of the glycan conformations between S-only and S-antibody systems reveals the roles of glycans in S-antibody binding. Polysaccharides 18-24 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 47-48 34013268-5 2021 Comparison of the glycan conformations between S-only and S-antibody systems reveals the roles of glycans in S-antibody binding. Polysaccharides 18-24 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 58-59 34013268-5 2021 Comparison of the glycan conformations between S-only and S-antibody systems reveals the roles of glycans in S-antibody binding. Polysaccharides 18-24 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 58-59 34013268-5 2021 Comparison of the glycan conformations between S-only and S-antibody systems reveals the roles of glycans in S-antibody binding. Polysaccharides 98-105 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 47-48 34013268-5 2021 Comparison of the glycan conformations between S-only and S-antibody systems reveals the roles of glycans in S-antibody binding. Polysaccharides 98-105 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 58-59 34013268-5 2021 Comparison of the glycan conformations between S-only and S-antibody systems reveals the roles of glycans in S-antibody binding. Polysaccharides 98-105 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 58-59 33903171-7 2021 Therefore, this glycan can interfere with the binding of the spike protein and protect against docking of the virus to the cell. Polysaccharides 16-22 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 61-66 33903171-8 2021 By contrast, the glycan at the N322 site interacts tightly with the RBD of the ACE2-bound spike protein and strengthens the complex. Polysaccharides 17-23 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 90-95 33689337-3 2021 In this work, multiple mus-long all-atom molecular dynamics simulations were performed to provide deeper insights into the structure and dynamics of S protein and glycan functions. Polysaccharides 163-169 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 149-150 33928117-0 2021 Glycans of SARS-CoV-2 Spike Protein in Virus Infection and Antibody Production. Polysaccharides 0-7 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 22-27 33605822-11 2021 Elucidation of the glycan repertoire on the spike protein can propel research for the development of an appropriate vaccine. Polysaccharides 19-25 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 44-49 33758835-5 2021 Molecular dynamics (MD) simulations of a fully glycosylated spike support s a model of steric restrictions that shape enzymatic processing of the glycans. Polysaccharides 146-153 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 60-65 33657316-0 2021 Heterogeneity of Glycan Processing on Trimeric SARS-CoV-2 Spike Protein Revealed by Charge Detection Mass Spectrometry. Polysaccharides 17-23 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 58-63 33838626-0 2021 Recombinant SARS-CoV-2 S Protein Binds to Glycans of the Lactosamine Family in vitro. Polysaccharides 42-49 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 12-13 33838626-3 2021 We studied interaction of the recombinant SARS-CoV-2 spike (S) protein with an array of glycoconjugates, including various sialylated, sulfated, and other glycans, and found that the S protein binds some (but not all) glycans of the lactosamine family. Polysaccharides 155-162 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 53-58 33838626-3 2021 We studied interaction of the recombinant SARS-CoV-2 spike (S) protein with an array of glycoconjugates, including various sialylated, sulfated, and other glycans, and found that the S protein binds some (but not all) glycans of the lactosamine family. Polysaccharides 155-162 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 42-43 33838626-3 2021 We studied interaction of the recombinant SARS-CoV-2 spike (S) protein with an array of glycoconjugates, including various sialylated, sulfated, and other glycans, and found that the S protein binds some (but not all) glycans of the lactosamine family. Polysaccharides 155-162 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 45-46 33838626-3 2021 We studied interaction of the recombinant SARS-CoV-2 spike (S) protein with an array of glycoconjugates, including various sialylated, sulfated, and other glycans, and found that the S protein binds some (but not all) glycans of the lactosamine family. Polysaccharides 218-225 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 53-58 33838626-3 2021 We studied interaction of the recombinant SARS-CoV-2 spike (S) protein with an array of glycoconjugates, including various sialylated, sulfated, and other glycans, and found that the S protein binds some (but not all) glycans of the lactosamine family. Polysaccharides 218-225 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 42-43 33838626-3 2021 We studied interaction of the recombinant SARS-CoV-2 spike (S) protein with an array of glycoconjugates, including various sialylated, sulfated, and other glycans, and found that the S protein binds some (but not all) glycans of the lactosamine family. Polysaccharides 218-225 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 45-46 33481336-3 2021 Human ACE2 is heavily glycosylated and its glycans impact on binding to the SARS-CoV-2 spike protein and virus infectivity. Polysaccharides 43-50 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 87-92 33340519-6 2021 We then probed the impact of ACE2 glycosylation on S binding and revealed a subtle sensitivity with hypersialylated or oligomannose-type glycans slightly impeding the interaction. Polysaccharides 137-144 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 51-52 32915505-1 2020 The glycan structures of the receptor binding domain of the SARS-CoV2 spike glycoprotein expressed in human HEK293F cells have been studied by using NMR. Polysaccharides 4-10 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 70-75 33495714-0 2021 Binding of the SARS-CoV-2 Spike Protein to Glycans. Polysaccharides 43-50 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 26-31 33495714-4 2021 In this study, we examined and compared the binding of the subunits and spike (S) proteins of SARS-CoV-2 and SARS-CoV, MERS-CoV to these glycans. Polysaccharides 137-144 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 72-77 33140034-3 2020 Similar to many other viral fusion proteins, the SARS-CoV-2 spike utilizes a glycan shield to thwart the host immune response. Polysaccharides 77-83 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 60-65 33140034-0 2020 Beyond Shielding: The Roles of Glycans in the SARS-CoV-2 Spike Protein. Polysaccharides 31-38 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 57-62 32363391-8 2020 The elucidation of the glycan repertoire on the spike protein provides insights into the viral binding studies and more importantly, propels research toward the development of a suitable vaccine candidate. Polysaccharides 23-29 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 48-53 33064451-0 2020 Comprehensive Analysis of the Glycan Complement of SARS-CoV-2 Spike Proteins Using Signature Ions-Triggered Electron-Transfer/Higher-Energy Collisional Dissociation (EThcD) Mass Spectrometry. Polysaccharides 30-36 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 62-67 33140034-8 2020 Additionally, end-to-end accessibility analyses outline a complete overview of the vulnerabilities of the glycan shield of the SARS-CoV-2 S protein, which may be exploited in the therapeutic efforts targeting this molecular machine. Polysaccharides 106-112 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 127-128 33140034-9 2020 Overall, this work presents hitherto unseen functional and structural insights into the SARS-CoV-2 S protein and its glycan coat, providing a strategy to control the conformational plasticity of the RBD that could be harnessed for vaccine development. Polysaccharides 117-123 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 88-89 32817270-5 2020 We propose that the hinges allow S to scan the host cell surface, shielded from antibodies by an extensive glycan coat. Polysaccharides 107-113 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 33-34 32929138-0 2020 Analysis of the SARS-CoV-2 spike protein glycan shield reveals implications for immune recognition. Polysaccharides 41-47 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 27-32 32841605-4 2020 Our results highlight roles for glycans in sterically masking polypeptide epitopes and directly modulating Spike-ACE2 interactions. Polysaccharides 32-39 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 107-112 32637953-4 2020 Here we demonstrate binding to the SARS-CoV-2 S protein by a category of Fab-dimerized glycan-reactive (FDG) HIV-1-induced broadly neutralizing antibodies (bnAbs). Polysaccharides 87-93 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 35-36 32944295-0 2020 Impact of glycan cloud on the B-cell epitope prediction of SARS-CoV-2 Spike protein. Polysaccharides 10-16 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 70-75 32944295-7 2020 We identify 28 B-cell epitopes in the Spike structure and group them as non-affected by the glycan cloud versus those which are strongly masked by the glycan cloud, resulting in a list of favourable epitopes as targets for vaccine development, antibody-based therapy and diagnostics. Polysaccharides 92-98 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 38-43 32944295-7 2020 We identify 28 B-cell epitopes in the Spike structure and group them as non-affected by the glycan cloud versus those which are strongly masked by the glycan cloud, resulting in a list of favourable epitopes as targets for vaccine development, antibody-based therapy and diagnostics. Polysaccharides 151-157 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 38-43 32904601-0 2021 Mass Spectrometry Analysis of Newly Emerging Coronavirus HCoV-19 Spike Protein and Human ACE2 Reveals Camouflaging Glycans and Unique Post-Translational Modifications. Polysaccharides 115-122 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 65-70 32366695-0 2020 Site-specific glycan analysis of the SARS-CoV-2 spike. Polysaccharides 14-20 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 48-53 32366695-5 2020 This analysis enables mapping of the glycan-processing states across the trimeric viral spike. Polysaccharides 37-43 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 88-93 34883069-0 2022 SARS-Cov-2 Spike binding to ACE2 is stronger and longer ranged due to glycan interaction. Polysaccharides 70-76 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 11-16 33236007-4 2020 We present several novel scientific discoveries, including the elucidation of the spike"s full glycan shield, the role of spike glycans in modulating the infectivity of the virus, and the characterization of the flexible interactions between the spike and the human ACE2 receptor. Polysaccharides 95-101 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 82-87 34278967-2 2021 S protein is heavily glycosylated and the glycosylation sites are relatively conserved, thus glycans on S protein surface could be a target for development of anti-SARS-CoV-2 strategies against variants. Polysaccharides 93-100 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 0-1 34742404-4 2022 Further, we show that homogeneous polysaccharide 37502 from the 375 may bind to 3CLpro well and disturb spike protein binding to ACE2 receptor. Polysaccharides 34-48 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 104-109 34925381-0 2021 Glycan Masking of Epitopes in the NTD and RBD of the Spike Protein Elicits Broadly Neutralizing Antibodies Against SARS-CoV-2 Variants. Polysaccharides 0-6 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 53-58 34869209-3 2021 Recent studies show that spike protein glycans play critical roles in viral entry and infection. Polysaccharides 39-46 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 25-30 34869209-16 2021 SARS-CoV-2 spike glycans are associated with host ACE2 receptor interaction efficiency. Polysaccharides 17-24 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 11-16 34213308-5 2021 Molecular dynamics simulations of a fully glycosylated spike support a model of steric restrictions that shape enzymatic processing of the glycans. Polysaccharides 139-146 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 55-60 34529436-5 2021 Comparison of the glycan conformations between S-only and S-antibody systems reveals the roles of glycans in S-antibody binding. Polysaccharides 18-24 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 47-48 34529436-5 2021 Comparison of the glycan conformations between S-only and S-antibody systems reveals the roles of glycans in S-antibody binding. Polysaccharides 18-24 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 58-59 34529436-5 2021 Comparison of the glycan conformations between S-only and S-antibody systems reveals the roles of glycans in S-antibody binding. Polysaccharides 18-24 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 109-110 34529436-5 2021 Comparison of the glycan conformations between S-only and S-antibody systems reveals the roles of glycans in S-antibody binding. Polysaccharides 98-105 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 47-48 34529436-5 2021 Comparison of the glycan conformations between S-only and S-antibody systems reveals the roles of glycans in S-antibody binding. Polysaccharides 98-105 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 58-59 34529436-5 2021 Comparison of the glycan conformations between S-only and S-antibody systems reveals the roles of glycans in S-antibody binding. Polysaccharides 98-105 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 109-110 34631661-11 2021 The relatively higher amount of high-mannose abundant sites (N17, N234, N343, N616, N709, N717, N801, and N1134) on HEK-Spike suggests that glycan-shielding may differ among the two constructs. Polysaccharides 140-146 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 120-125 34735575-1 2022 Extensive glycosylation of the spike protein of severe acute respiratory syndrome coronavirus 2 virus not only shields the major part of it from host immune responses, but glycans at specific sites also act on its conformation dynamics and contribute to efficient host receptor binding, and hence infectivity. Polysaccharides 172-179 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 31-36 34452053-1 2021 The Receptor-Binding Domain (RBD) of the Spike (S) protein from Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) has glycosylation sites which can limit the production of reliable antigens expressed in prokaryotic platforms, due to glycan-mediated evasion of the host immune response. Polysaccharides 244-250 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 41-46 34452053-1 2021 The Receptor-Binding Domain (RBD) of the Spike (S) protein from Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) has glycosylation sites which can limit the production of reliable antigens expressed in prokaryotic platforms, due to glycan-mediated evasion of the host immune response. Polysaccharides 244-250 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 48-49 34328324-2 2021 However, the molecular structures and glycan heterogeneity of the new O-glycans found on the S protein regional-binding domain (S-RBD) remain cryptic because of the challenges in intact glycoform analysis by conventional bottom-up glycoproteomic approaches. Polysaccharides 38-44 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 128-129 34375000-6 2021 3D modelling showed that both lectins can bind to a glycan within the RBD-ACE2 interface and thus interferes with Spike binding to cell surfaces. Polysaccharides 52-58 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 114-119 34413500-0 2021 A glycan gate controls opening of the SARS-CoV-2 spike protein. Polysaccharides 2-8 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 49-54 34413500-1 2021 SARS-CoV-2 infection is controlled by the opening of the spike protein receptor binding domain (RBD), which transitions from a glycan-shielded "down" to an exposed "up" state to bind the human angiotensin-converting enzyme 2 receptor and infect cells. Polysaccharides 127-133 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 57-62 34463614-7 2021 Interestingly, the Spike protein possesses many post-translational modifications, in the form of branched glycans that flank the surface of the assembly. Polysaccharides 106-113 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 19-24 34463614-10 2021 These simulations indicate that the steric composition of the glycans can induce a pause during the Spike protein conformational change. Polysaccharides 62-69 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 100-105 34238357-0 2021 A bivalent protein targeting glycans and HR1 domain in spike protein potently inhibited infection of SARS-CoV-2 and other human coronaviruses. Polysaccharides 29-36 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 55-60 35332581-4 2022 Herein, we rationally developed a nanoparticle vaccine, termed SCTV01B, by using the capsular polysaccharide of S. pneumoniae serotype 14 (PPS14) as the backbone to conjugate with the recombinant receptor binding domain (RBD) of the SARS-CoV-2 spike protein. Polysaccharides 94-108 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 244-249 34127709-0 2021 Glycan reactive anti-HIV-1 antibodies bind the SARS-CoV-2 spike protein but do not block viral entry. Polysaccharides 0-6 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 58-63 34127709-2 2021 A common feature amongst enveloped viruses such as SARS-CoV-2 and HIV-1 is the propensity for displaying host-derived glycans on entry spike proteins. Polysaccharides 118-125 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 135-140 34127709-6 2021 Nevertheless, ELISA and other immunoreactivity experiments demonstrate these antibodies are capable of binding the SARS-CoV-2 spike in a glycan-dependent manner. Polysaccharides 137-143 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 126-131 35562647-10 2022 Lectibodies can lead to neutralization and clearance of viruses and cells infected by viruses by binding to glycans located on the envelope surface (e.g., the heavily glycosylated SARS-CoV-2 spike protein). Polysaccharides 108-115 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 191-196 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. Polysaccharides 75-82 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 110-115 35475171-0 2022 Distinct Core Glycan and O-Glycoform Utilization of SARS-CoV-2 Omicron Variant Spike Protein RBD Revealed by Top-Down Mass Spectrometry. Polysaccharides 14-20 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 79-84 35495643-0 2022 Assessing the Mobility of Severe Acute Respiratory Syndrome Coronavirus-2 Spike Protein Glycans by Structural and Computational Methods. Polysaccharides 88-95 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 74-79 35495643-3 2022 Like to many other viral fusion proteins, the SARS-CoV-2 spike protein utilizes a glycan shield to thwart the host immune response. Polysaccharides 82-88 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 57-62 35230146-0 2022 Vaccination with SARS-CoV-2 spike protein lacking glycan shields elicits enhanced protective responses in animal models. Polysaccharides 50-56 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 28-33 35230146-2 2022 As the key immunogen, the viral surface spike (S) protein is frequently mutated, and conserved epitopes are shielded by glycans. Polysaccharides 120-127 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 40-45 35230146-2 2022 As the key immunogen, the viral surface spike (S) protein is frequently mutated, and conserved epitopes are shielded by glycans. Polysaccharides 120-127 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 47-48 35102342-4 2022 MBL bound trimeric spike protein, including that of variants of concern (VoC), in a glycan-dependent manner and inhibited SARS-CoV-2 in three in vitro models. Polysaccharides 84-90 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 19-24 35112841-4 2022 Herein, we report that CUR-encapsulated polysaccharide nanoparticles (CUR-PS-NPs) potently inhibit the release of cytokines, chemokines, and growth factors associated with damage of SARS-CoV-2 spike protein (CoV2-SP)-stimulated liver Huh7.5 and lung A549 epithelial cells. Polysaccharides 40-54 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 193-198 35215371-5 2022 In the current study, a small library of sulfated glycans and highly negatively charged compounds, including pentosan polysulfate (PPS), mucopolysaccharide polysulfate (MPS), sulfated lactobionic acid, sulodexide, and defibrotide, was assembled and evaluated for binding to the S-proteins and inhibition of viral infectivity in vitro. Polysaccharides 50-57 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 278-279 35178379-2 2021 The SARS-CoV-2 spike protein is heavily glycosylated and host-derived glycan modifications contribute to the formation of specific immunogenic epitopes, enhance the virus-cell interaction or affect virus transmission. Polysaccharides 70-76 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 15-20