Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-119 |
Sentence |
denotes |
Quantifying the binding stoichiometry and affinity of histo-blood group antigen oligosaccharides for human noroviruses. |
TextSentencer_T2 |
120-190 |
Sentence |
denotes |
Human noroviruses (HuNoVs) are a major cause of acute gastroenteritis. |
TextSentencer_T3 |
191-306 |
Sentence |
denotes |
Many HuNoVs recognize histo-blood group antigens (HBGAs) as cellular receptors or attachment factors for infection. |
TextSentencer_T4 |
307-485 |
Sentence |
denotes |
It was recently proposed that HuNoV recognition of HBGAs involves a cooperative, multistep binding mechanism that exploits both known and previously unknown glycan binding sites. |
TextSentencer_T5 |
486-1004 |
Sentence |
denotes |
In this study, binding measurements, implemented using electrospray ionization mass spectrometry (ESI-MS) were performed on homodimers of the protruding domain (P dimers) of the capsid protein of three HuNoV strains [Saga (GII.4), Vietnam 026 (GII.10) and VA387 (GII.4)] with the ethyl glycoside of the B trisaccharide (α-d-Gal-(1→3)-[α-l-Fuc-(1→2)]-β-d-Gal-OC2H5) and free B type 1 tetrasaccharide (α-d-Gal-(1→3)-[α-l-Fuc-(1→2)]-β-d-Gal-(1→3)-d-GlcNAc) in an effort to confirm the existence of new HBGA binding sites. |
TextSentencer_T6 |
1005-1239 |
Sentence |
denotes |
After correcting the mass spectra for nonspecific interactions that form in ESI droplets as they evaporate to dryness, all three P dimers were found to bind a maximum of two B trisaccharides at the highest concentrations investigated. |
TextSentencer_T7 |
1240-1344 |
Sentence |
denotes |
The apparent affinities measured for stepwise binding of B trisaccharide suggest positive cooperativity. |
TextSentencer_T8 |
1345-1428 |
Sentence |
denotes |
Similar results were obtained for B type 1 tetrasaccharide binding to Saga P dimer. |
TextSentencer_T9 |
1429-1524 |
Sentence |
denotes |
Based on these results, it is proposed that HuNoV P dimers possess only two HBGA binding sites. |
TextSentencer_T10 |
1525-1800 |
Sentence |
denotes |
It is also shown that nonspecific binding corrections applied to mass spectra acquired using energetic ion source conditions that promote in-source dissociation can lead to apparent HuNoV-HBGA oligosaccharide binding stoichiometries and affinities that are artificially high. |
TextSentencer_T11 |
1801-1928 |
Sentence |
denotes |
Finally, evidence that high concentrations of oligosaccharide can induce conformational changes in HuNoV P dimers is presented. |
T1 |
0-119 |
Sentence |
denotes |
Quantifying the binding stoichiometry and affinity of histo-blood group antigen oligosaccharides for human noroviruses. |
T2 |
120-190 |
Sentence |
denotes |
Human noroviruses (HuNoVs) are a major cause of acute gastroenteritis. |
T3 |
191-306 |
Sentence |
denotes |
Many HuNoVs recognize histo-blood group antigens (HBGAs) as cellular receptors or attachment factors for infection. |
T4 |
307-485 |
Sentence |
denotes |
It was recently proposed that HuNoV recognition of HBGAs involves a cooperative, multistep binding mechanism that exploits both known and previously unknown glycan binding sites. |
T5 |
486-1004 |
Sentence |
denotes |
In this study, binding measurements, implemented using electrospray ionization mass spectrometry (ESI-MS) were performed on homodimers of the protruding domain (P dimers) of the capsid protein of three HuNoV strains [Saga (GII.4), Vietnam 026 (GII.10) and VA387 (GII.4)] with the ethyl glycoside of the B trisaccharide (α-d-Gal-(1→3)-[α-l-Fuc-(1→2)]-β-d-Gal-OC2H5) and free B type 1 tetrasaccharide (α-d-Gal-(1→3)-[α-l-Fuc-(1→2)]-β-d-Gal-(1→3)-d-GlcNAc) in an effort to confirm the existence of new HBGA binding sites. |
T6 |
1005-1239 |
Sentence |
denotes |
After correcting the mass spectra for nonspecific interactions that form in ESI droplets as they evaporate to dryness, all three P dimers were found to bind a maximum of two B trisaccharides at the highest concentrations investigated. |
T7 |
1240-1344 |
Sentence |
denotes |
The apparent affinities measured for stepwise binding of B trisaccharide suggest positive cooperativity. |
T8 |
1345-1428 |
Sentence |
denotes |
Similar results were obtained for B type 1 tetrasaccharide binding to Saga P dimer. |
T9 |
1429-1524 |
Sentence |
denotes |
Based on these results, it is proposed that HuNoV P dimers possess only two HBGA binding sites. |
T10 |
1525-1800 |
Sentence |
denotes |
It is also shown that nonspecific binding corrections applied to mass spectra acquired using energetic ion source conditions that promote in-source dissociation can lead to apparent HuNoV-HBGA oligosaccharide binding stoichiometries and affinities that are artificially high. |
T11 |
1801-1928 |
Sentence |
denotes |
Finally, evidence that high concentrations of oligosaccharide can induce conformational changes in HuNoV P dimers is presented. |