Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-111 |
Sentence |
denotes |
Glycoengineering of alphaGal xenoantigen on recombinant peptide bearing the J28 pancreatic oncofetal glycotope. |
TextSentencer_T2 |
112-310 |
Sentence |
denotes |
In human pancreatic adenocarcinoma, alterations of glycosylation processes leads to the expression of tumor-associated carbohydrate antigens, representing potential targets for cancer immunotherapy. |
TextSentencer_T3 |
311-611 |
Sentence |
denotes |
Among these pancreatic tumor-associated carbohydrate antigens, the J28 glycotope located within the O-glycosylated mucin-like C-terminal domain of the fetoacinar pancreatic protein (FAPP) and expressed at the surface of human tumoral tissues, can be a good target for anticancer therapeutic vaccines. |
TextSentencer_T4 |
612-824 |
Sentence |
denotes |
However, the oncodevelopmental self character of the J28 glycotope associated with the low immunogenicity of tumor-associated carbohydrate antigens may be a major obstacle to effective anti-tumor vaccine therapy. |
TextSentencer_T5 |
825-1098 |
Sentence |
denotes |
In this study, we have investigated a method to increase the immunogenicity of the recombinant pancreatic oncofetal J28 glycotope by glycoengineering Galalpha1,3Galss1,4GlcNAc-R (alphaGal epitope) which may be recognized by natural anti-alphaGal antibody present in humans. |
TextSentencer_T6 |
1099-1277 |
Sentence |
denotes |
For this purpose, we have developed a stable Chinese hamster ovary cell clone expressing the alphaGal epitope by transfecting the cDNA encoding the alpha1,3galactosyltransferase. |
TextSentencer_T7 |
1278-1415 |
Sentence |
denotes |
These cells have been previously equipped to produce the recombinant O-glycosylated C-terminal domain of FAPP carrying the J28 glycotope. |
TextSentencer_T8 |
1416-1581 |
Sentence |
denotes |
As a consequence, the C-terminal domain of FAPP produced by these cells carries the alphaGal epitope on oligosaccharide structures associated with the J28 glycotope. |
TextSentencer_T9 |
1582-1850 |
Sentence |
denotes |
Furthermore, we show that this recombinant "alpha1,3galactosyl and J28 glycotope" may not only be targeted by human natural anti-alphaGal antibodies but also by the mAbJ28, suggesting that the J28 glycotope remains accessible to the immune system as vaccinating agent. |
TextSentencer_T10 |
1851-2062 |
Sentence |
denotes |
This approach may be used for many identified tumor-associated carbohydrate antigens which can be glycoengineered to carry a alphaGal epitope to increase their immunogenicity and to develop therapeutic vaccines. |
T1 |
0-111 |
Sentence |
denotes |
Glycoengineering of alphaGal xenoantigen on recombinant peptide bearing the J28 pancreatic oncofetal glycotope. |
T2 |
112-310 |
Sentence |
denotes |
In human pancreatic adenocarcinoma, alterations of glycosylation processes leads to the expression of tumor-associated carbohydrate antigens, representing potential targets for cancer immunotherapy. |
T3 |
311-611 |
Sentence |
denotes |
Among these pancreatic tumor-associated carbohydrate antigens, the J28 glycotope located within the O-glycosylated mucin-like C-terminal domain of the fetoacinar pancreatic protein (FAPP) and expressed at the surface of human tumoral tissues, can be a good target for anticancer therapeutic vaccines. |
T4 |
612-824 |
Sentence |
denotes |
However, the oncodevelopmental self character of the J28 glycotope associated with the low immunogenicity of tumor-associated carbohydrate antigens may be a major obstacle to effective anti-tumor vaccine therapy. |
T5 |
825-1098 |
Sentence |
denotes |
In this study, we have investigated a method to increase the immunogenicity of the recombinant pancreatic oncofetal J28 glycotope by glycoengineering Galalpha1,3Galss1,4GlcNAc-R (alphaGal epitope) which may be recognized by natural anti-alphaGal antibody present in humans. |
T6 |
1099-1277 |
Sentence |
denotes |
For this purpose, we have developed a stable Chinese hamster ovary cell clone expressing the alphaGal epitope by transfecting the cDNA encoding the alpha1,3galactosyltransferase. |
T7 |
1278-1415 |
Sentence |
denotes |
These cells have been previously equipped to produce the recombinant O-glycosylated C-terminal domain of FAPP carrying the J28 glycotope. |
T8 |
1416-1581 |
Sentence |
denotes |
As a consequence, the C-terminal domain of FAPP produced by these cells carries the alphaGal epitope on oligosaccharide structures associated with the J28 glycotope. |
T9 |
1582-1850 |
Sentence |
denotes |
Furthermore, we show that this recombinant "alpha1,3galactosyl and J28 glycotope" may not only be targeted by human natural anti-alphaGal antibodies but also by the mAbJ28, suggesting that the J28 glycotope remains accessible to the immune system as vaccinating agent. |
T10 |
1851-2062 |
Sentence |
denotes |
This approach may be used for many identified tumor-associated carbohydrate antigens which can be glycoengineered to carry a alphaGal epitope to increase their immunogenicity and to develop therapeutic vaccines. |
T1 |
0-111 |
Sentence |
denotes |
Glycoengineering of alphaGal xenoantigen on recombinant peptide bearing the J28 pancreatic oncofetal glycotope. |
T2 |
112-310 |
Sentence |
denotes |
In human pancreatic adenocarcinoma, alterations of glycosylation processes leads to the expression of tumor-associated carbohydrate antigens, representing potential targets for cancer immunotherapy. |
T3 |
311-611 |
Sentence |
denotes |
Among these pancreatic tumor-associated carbohydrate antigens, the J28 glycotope located within the O-glycosylated mucin-like C-terminal domain of the fetoacinar pancreatic protein (FAPP) and expressed at the surface of human tumoral tissues, can be a good target for anticancer therapeutic vaccines. |
T4 |
612-824 |
Sentence |
denotes |
However, the oncodevelopmental self character of the J28 glycotope associated with the low immunogenicity of tumor-associated carbohydrate antigens may be a major obstacle to effective anti-tumor vaccine therapy. |
T5 |
825-1098 |
Sentence |
denotes |
In this study, we have investigated a method to increase the immunogenicity of the recombinant pancreatic oncofetal J28 glycotope by glycoengineering Galalpha1,3Galss1,4GlcNAc-R (alphaGal epitope) which may be recognized by natural anti-alphaGal antibody present in humans. |
T6 |
1099-1277 |
Sentence |
denotes |
For this purpose, we have developed a stable Chinese hamster ovary cell clone expressing the alphaGal epitope by transfecting the cDNA encoding the alpha1,3galactosyltransferase. |
T7 |
1278-1415 |
Sentence |
denotes |
These cells have been previously equipped to produce the recombinant O-glycosylated C-terminal domain of FAPP carrying the J28 glycotope. |
T8 |
1416-1581 |
Sentence |
denotes |
As a consequence, the C-terminal domain of FAPP produced by these cells carries the alphaGal epitope on oligosaccharide structures associated with the J28 glycotope. |
T9 |
1582-1850 |
Sentence |
denotes |
Furthermore, we show that this recombinant "alpha1,3galactosyl and J28 glycotope" may not only be targeted by human natural anti-alphaGal antibodies but also by the mAbJ28, suggesting that the J28 glycotope remains accessible to the immune system as vaccinating agent. |
T10 |
1851-2062 |
Sentence |
denotes |
This approach may be used for many identified tumor-associated carbohydrate antigens which can be glycoengineered to carry a alphaGal epitope to increase their immunogenicity and to develop therapeutic vaccines. |