Id |
Subject |
Object |
Predicate |
Lexical cue |
T1 |
0-169 |
Sentence |
denotes |
Identification of 22 N-glycosites on spike glycoprotein of SARS-CoV-2 and accessible surface glycopeptide motifs: implications for vaccination and antibody therapeutics. |
T1 |
0-169 |
Sentence |
denotes |
Identification of 22 N-glycosites on spike glycoprotein of SARS-CoV-2 and accessible surface glycopeptide motifs: implications for vaccination and antibody therapeutics. |
T2 |
170-261 |
Sentence |
denotes |
Coronaviruses hijack human enzymes to assemble the sugar coat on their spike glycoproteins. |
T2 |
170-261 |
Sentence |
denotes |
Coronaviruses hijack human enzymes to assemble the sugar coat on their spike glycoproteins. |
T3 |
262-391 |
Sentence |
denotes |
The mechanisms by which human antibodies may recognize the antigenic viral peptide epitopes hidden by the sugar coat are unknown. |
T3 |
262-391 |
Sentence |
denotes |
The mechanisms by which human antibodies may recognize the antigenic viral peptide epitopes hidden by the sugar coat are unknown. |
T4 |
392-577 |
Sentence |
denotes |
Glycosylation by insect cells differs from the native form produced in human cells, but insect cell-derived influenza vaccines have been approved by the US Food and Drug Administration. |
T4 |
392-577 |
Sentence |
denotes |
Glycosylation by insect cells differs from the native form produced in human cells, but insect cell-derived influenza vaccines have been approved by the US Food and Drug Administration. |
T5 |
578-810 |
Sentence |
denotes |
In this study, we analyzed recombinant severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein secreted from BTI-Tn-5B1-4 insect cells, by trypsin and chymotrypsin digestion followed by mass spectrometry analysis. |
T5 |
578-810 |
Sentence |
denotes |
In this study, we analyzed recombinant severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein secreted from BTI-Tn-5B1-4 insect cells, by trypsin and chymotrypsin digestion followed by mass spectrometry analysis. |
T6 |
811-925 |
Sentence |
denotes |
We acquired tandem mass spectrometry (MS/MS) spectrums for glycopeptides of all 22 predicted N-glycosylated sites. |
T6 |
811-925 |
Sentence |
denotes |
We acquired tandem mass spectrometry (MS/MS) spectrums for glycopeptides of all 22 predicted N-glycosylated sites. |
T7 |
926-1114 |
Sentence |
denotes |
We further analyzed the surface accessibility of spike proteins according to cryogenic electron microscopy and homolog-modeled structures, and available antibodies that bind to SARS-CoV-1. |
T7 |
926-1114 |
Sentence |
denotes |
We further analyzed the surface accessibility of spike proteins according to cryogenic electron microscopy and homolog-modeled structures, and available antibodies that bind to SARS-CoV-1. |
T8 |
1115-1196 |
Sentence |
denotes |
All 22 N-glycosylated sites of SARS-CoV-2 are modified by high-mannose N-glycans. |
T8 |
1115-1196 |
Sentence |
denotes |
All 22 N-glycosylated sites of SARS-CoV-2 are modified by high-mannose N-glycans. |
T9 |
1197-1265 |
Sentence |
denotes |
MS/MS fragmentation clearly established the glycopeptide identities. |
T9 |
1197-1265 |
Sentence |
denotes |
MS/MS fragmentation clearly established the glycopeptide identities. |
T10 |
1266-1470 |
Sentence |
denotes |
Electron densities of glycans cover most of the spike receptor-binding domain of SARS-CoV-2, except YQAGSTPCNGVEGFNCYFPLQSYGFQPTNGVGYQ, similar to a region FSPDGKPCTPPALNCYWPLNDYGFYTTTGIGYQ in SARS-CoV-1. |
T10 |
1266-1470 |
Sentence |
denotes |
Electron densities of glycans cover most of the spike receptor-binding domain of SARS-CoV-2, except YQAGSTPCNGVEGFNCYFPLQSYGFQPTNGVGYQ, similar to a region FSPDGKPCTPPALNCYWPLNDYGFYTTTGIGYQ in SARS-CoV-1. |
T11 |
1471-1598 |
Sentence |
denotes |
Other surface-exposed domains include those located on central helix, connecting region, heptad repeats, and N-terminal domain. |
T11 |
1471-1598 |
Sentence |
denotes |
Other surface-exposed domains include those located on central helix, connecting region, heptad repeats, and N-terminal domain. |
T12 |
1599-1917 |
Sentence |
denotes |
Because the majority of antibody paratopes bind to the peptide portion with or without sugar modification, we propose a snake-catching model for predicted paratopes: a minimal length of peptide is first clamped by a paratope, and sugar modifications close to the peptide either strengthen or do not hinder the binding. |
T12 |
1599-1917 |
Sentence |
denotes |
Because the majority of antibody paratopes bind to the peptide portion with or without sugar modification, we propose a snake-catching model for predicted paratopes: a minimal length of peptide is first clamped by a paratope, and sugar modifications close to the peptide either strengthen or do not hinder the binding. |