| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-126 |
Sentence |
denotes |
Characterization of host-cell line specific glycosylation profiles of early transmitted/founder HIV-1 gp120 envelope proteins. |
| T1 |
0-126 |
Sentence |
denotes |
Characterization of host-cell line specific glycosylation profiles of early transmitted/founder HIV-1 gp120 envelope proteins. |
| TextSentencer_T2 |
127-261 |
Sentence |
denotes |
Glycosylation plays an essential role in regulating protein function by modulating biological, structural, and therapeutic properties. |
| T2 |
127-261 |
Sentence |
denotes |
Glycosylation plays an essential role in regulating protein function by modulating biological, structural, and therapeutic properties. |
| TextSentencer_T3 |
262-392 |
Sentence |
denotes |
However, due to its inherent heterogeneity and diversity, the comprehensive analysis of protein glycosylation remains a challenge. |
| T3 |
262-392 |
Sentence |
denotes |
However, due to its inherent heterogeneity and diversity, the comprehensive analysis of protein glycosylation remains a challenge. |
| TextSentencer_T4 |
393-798 |
Sentence |
denotes |
As part of our continuing effort in the analysis of glycosylation profiles of recombinant HIV-1 envelope-based immunogens, we evaluated and compared the host-cell specific glycosylation pattern of recombinant HIV-1 surface glycoprotein, gp120, derived from clade C transmitted/founder virus 1086.C expressed in Chinese hamster ovary (CHO) and human embryonic kidney containing T antigen (293T) cell lines. |
| T4 |
393-798 |
Sentence |
denotes |
As part of our continuing effort in the analysis of glycosylation profiles of recombinant HIV-1 envelope-based immunogens, we evaluated and compared the host-cell specific glycosylation pattern of recombinant HIV-1 surface glycoprotein, gp120, derived from clade C transmitted/founder virus 1086.C expressed in Chinese hamster ovary (CHO) and human embryonic kidney containing T antigen (293T) cell lines. |
| TextSentencer_T5 |
799-1071 |
Sentence |
denotes |
We used an integrated glycopeptide-based mass mapping workflow that includes a partial deglycosylation step described in our previous study with the inclusion of a fragmentation technique, electron transfer dissociation (ETD), to complement collision-induced dissociation. |
| T5 |
799-1071 |
Sentence |
denotes |
We used an integrated glycopeptide-based mass mapping workflow that includes a partial deglycosylation step described in our previous study with the inclusion of a fragmentation technique, electron transfer dissociation (ETD), to complement collision-induced dissociation. |
| TextSentencer_T6 |
1072-1274 |
Sentence |
denotes |
The inclusion of ETD facilitated the analysis by providing additional validation for glycopeptide identification and expanding the identified glycopeptides to include coverage of O-linked glycosylation. |
| T6 |
1072-1274 |
Sentence |
denotes |
The inclusion of ETD facilitated the analysis by providing additional validation for glycopeptide identification and expanding the identified glycopeptides to include coverage of O-linked glycosylation. |
| TextSentencer_T7 |
1275-1438 |
Sentence |
denotes |
The site-specific glycosylation analysis shows that the transmitted/founder 1086.C gp120 expressed in CHO and 293T displayed distinct similarities and differences. |
| T7 |
1275-1438 |
Sentence |
denotes |
The site-specific glycosylation analysis shows that the transmitted/founder 1086.C gp120 expressed in CHO and 293T displayed distinct similarities and differences. |
| TextSentencer_T8 |
1439-1697 |
Sentence |
denotes |
For N-linked glycosylation, two sites (N386 and N392) in the V4 region were populated with high mannose glycans in the CHO cell-derived 1086.C gp120, while these sites had a mixture of high mannose and processed glycans in the 293T cell-derived 1086.C gp120. |
| T8 |
1439-1697 |
Sentence |
denotes |
For N-linked glycosylation, two sites (N386 and N392) in the V4 region were populated with high mannose glycans in the CHO cell-derived 1086.C gp120, while these sites had a mixture of high mannose and processed glycans in the 293T cell-derived 1086.C gp120. |
| TextSentencer_T9 |
1698-1923 |
Sentence |
denotes |
Compositional analysis of O-linked glycans revealed that 293T cell-derived 1086.C gp120 consisted of core 1, 2, and 4 type O-linked glycans, while CHO cell-derived 1086.C exclusively consisted of core 1 type O-linked glycans. |
| T9 |
1698-1923 |
Sentence |
denotes |
Compositional analysis of O-linked glycans revealed that 293T cell-derived 1086.C gp120 consisted of core 1, 2, and 4 type O-linked glycans, while CHO cell-derived 1086.C exclusively consisted of core 1 type O-linked glycans. |
| TextSentencer_T10 |
1924-2087 |
Sentence |
denotes |
Overall, glycosylation site occupancy of the CHO and 293T cell-derived 1086.C gp120 showed a high degree of similarity except for one site at N88 in the C1 region. |
| T10 |
1924-2087 |
Sentence |
denotes |
Overall, glycosylation site occupancy of the CHO and 293T cell-derived 1086.C gp120 showed a high degree of similarity except for one site at N88 in the C1 region. |
| TextSentencer_T11 |
2088-2167 |
Sentence |
denotes |
This site was partially occupied in 293T-gp120 but fully occupied in CHO-gp120. |
| T11 |
2088-2167 |
Sentence |
denotes |
This site was partially occupied in 293T-gp120 but fully occupied in CHO-gp120. |
| TextSentencer_T12 |
2168-2382 |
Sentence |
denotes |
Site-specific glycopeptide analysis of transmitted/founder 1086.C gp120 expressed in CHO cells revealed the presence of phosphorylated glycans, while 293T cell-produced 1086.C gp120 glycans were not phosphorylated. |
| T12 |
2168-2382 |
Sentence |
denotes |
Site-specific glycopeptide analysis of transmitted/founder 1086.C gp120 expressed in CHO cells revealed the presence of phosphorylated glycans, while 293T cell-produced 1086.C gp120 glycans were not phosphorylated. |
| TextSentencer_T13 |
2383-2615 |
Sentence |
denotes |
While the influence of phosphorylated glycans on immunogenicity is unclear, distinguishing host-cell specific variations in glycosylation profiles provide insights into the similarity (or difference) in recombinant vaccine products. |
| T13 |
2383-2615 |
Sentence |
denotes |
While the influence of phosphorylated glycans on immunogenicity is unclear, distinguishing host-cell specific variations in glycosylation profiles provide insights into the similarity (or difference) in recombinant vaccine products. |
| TextSentencer_T14 |
2616-2837 |
Sentence |
denotes |
While these differences had minimal effect on envelope antigenicity, they may be important in considering immunogenicity and functional capacities of recombinant envelope proteins produced in different expression systems. |
| T14 |
2616-2837 |
Sentence |
denotes |
While these differences had minimal effect on envelope antigenicity, they may be important in considering immunogenicity and functional capacities of recombinant envelope proteins produced in different expression systems. |