High throughput isolation and glycosylation analysis of IgG-variability and heritability of the IgG glycome in three isolated human populations
All immunoglobulin G molecules carry N-glycans, which modulate their biological activity. Changes in N-glycosylation of IgG associate with various diseases and affect the activity of therapeutic antibodies and intravenous immunoglobulins. We have developed a novel 96-well protein G monolithic plate...
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| Veröffentlicht in: | Molecular & cellular proteomics Jg. 10; H. 10; S. M111.010090 |
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| Format: | Journal Article |
| Sprache: | Englisch |
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01.10.2011
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| ISSN: | 1535-9484, 1535-9484 |
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| Abstract | All immunoglobulin G molecules carry N-glycans, which modulate their biological activity. Changes in N-glycosylation of IgG associate with various diseases and affect the activity of therapeutic antibodies and intravenous immunoglobulins. We have developed a novel 96-well protein G monolithic plate and used it to rapidly isolate IgG from plasma of 2298 individuals from three isolated human populations. N-glycans were released by PNGase F, labeled with 2-aminobenzamide and analyzed by hydrophilic interaction chromatography with fluorescence detection. The majority of the structural features of the IgG glycome were consistent with previous studies, but sialylation was somewhat higher than reported previously. Sialylation was particularly prominent in core fucosylated glycans containing two galactose residues and bisecting GlcNAc where median sialylation level was nearly 80%. Very high variability between individuals was observed, approximately three times higher than in the total plasma glycome. For example, neutral IgG glycans without core fucose varied between 1.3 and 19%, a difference that significantly affects the effector functions of natural antibodies, predisposing or protecting individuals from particular diseases. Heritability of IgG glycans was generally between 30 and 50%. The individual's age was associated with a significant decrease in galactose and increase of bisecting GlcNAc, whereas other functional elements of IgG glycosylation did not change much with age. Gender was not an important predictor for any IgG glycan. An important observation is that competition between glycosyltransferases, which occurs in vitro, did not appear to be relevant in vivo, indicating that the final glycan structures are not a simple result of competing enzymatic activities, but a carefully regulated outcome designed to meet the prevailing physiological needs. |
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| AbstractList | All immunoglobulin G molecules carry N-glycans, which modulate their biological activity. Changes in N-glycosylation of IgG associate with various diseases and affect the activity of therapeutic antibodies and intravenous immunoglobulins. We have developed a novel 96-well protein G monolithic plate and used it to rapidly isolate IgG from plasma of 2298 individuals from three isolated human populations. N-glycans were released by PNGase F, labeled with 2-aminobenzamide and analyzed by hydrophilic interaction chromatography with fluorescence detection. The majority of the structural features of the IgG glycome were consistent with previous studies, but sialylation was somewhat higher than reported previously. Sialylation was particularly prominent in core fucosylated glycans containing two galactose residues and bisecting GlcNAc where median sialylation level was nearly 80%. Very high variability between individuals was observed, approximately three times higher than in the total plasma glycome. For example, neutral IgG glycans without core fucose varied between 1.3 and 19%, a difference that significantly affects the effector functions of natural antibodies, predisposing or protecting individuals from particular diseases. Heritability of IgG glycans was generally between 30 and 50%. The individual's age was associated with a significant decrease in galactose and increase of bisecting GlcNAc, whereas other functional elements of IgG glycosylation did not change much with age. Gender was not an important predictor for any IgG glycan. An important observation is that competition between glycosyltransferases, which occurs in vitro, did not appear to be relevant in vivo, indicating that the final glycan structures are not a simple result of competing enzymatic activities, but a carefully regulated outcome designed to meet the prevailing physiological needs.All immunoglobulin G molecules carry N-glycans, which modulate their biological activity. Changes in N-glycosylation of IgG associate with various diseases and affect the activity of therapeutic antibodies and intravenous immunoglobulins. We have developed a novel 96-well protein G monolithic plate and used it to rapidly isolate IgG from plasma of 2298 individuals from three isolated human populations. N-glycans were released by PNGase F, labeled with 2-aminobenzamide and analyzed by hydrophilic interaction chromatography with fluorescence detection. The majority of the structural features of the IgG glycome were consistent with previous studies, but sialylation was somewhat higher than reported previously. Sialylation was particularly prominent in core fucosylated glycans containing two galactose residues and bisecting GlcNAc where median sialylation level was nearly 80%. Very high variability between individuals was observed, approximately three times higher than in the total plasma glycome. For example, neutral IgG glycans without core fucose varied between 1.3 and 19%, a difference that significantly affects the effector functions of natural antibodies, predisposing or protecting individuals from particular diseases. Heritability of IgG glycans was generally between 30 and 50%. The individual's age was associated with a significant decrease in galactose and increase of bisecting GlcNAc, whereas other functional elements of IgG glycosylation did not change much with age. Gender was not an important predictor for any IgG glycan. An important observation is that competition between glycosyltransferases, which occurs in vitro, did not appear to be relevant in vivo, indicating that the final glycan structures are not a simple result of competing enzymatic activities, but a carefully regulated outcome designed to meet the prevailing physiological needs. All immunoglobulin G molecules carry N-glycans, which modulate their biological activity. Changes in N-glycosylation of IgG associate with various diseases and affect the activity of therapeutic antibodies and intravenous immunoglobulins. We have developed a novel 96-well protein G monolithic plate and used it to rapidly isolate IgG from plasma of 2298 individuals from three isolated human populations. N-glycans were released by PNGase F, labeled with 2-aminobenzamide and analyzed by hydrophilic interaction chromatography with fluorescence detection. The majority of the structural features of the IgG glycome were consistent with previous studies, but sialylation was somewhat higher than reported previously. Sialylation was particularly prominent in core fucosylated glycans containing two galactose residues and bisecting GlcNAc where median sialylation level was nearly 80%. Very high variability between individuals was observed, approximately three times higher than in the total plasma glycome. For example, neutral IgG glycans without core fucose varied between 1.3 and 19%, a difference that significantly affects the effector functions of natural antibodies, predisposing or protecting individuals from particular diseases. Heritability of IgG glycans was generally between 30 and 50%. The individual's age was associated with a significant decrease in galactose and increase of bisecting GlcNAc, whereas other functional elements of IgG glycosylation did not change much with age. Gender was not an important predictor for any IgG glycan. An important observation is that competition between glycosyltransferases, which occurs in vitro, did not appear to be relevant in vivo, indicating that the final glycan structures are not a simple result of competing enzymatic activities, but a carefully regulated outcome designed to meet the prevailing physiological needs. |
| Author | Polasek, Ozren Rudan, Igor Pucić, Maja Campbell, Harry Vidic, Jana Rudd, Pauline M Knezević, Ana Josić, Djuro Hastie, Nicholas D Gornik, Olga Novokmet, Mislav Supraha-Goreta, Sandra Wright, Alan Redzić, Irma Wormald, Mark R Wuhrer, Manfred Adamczyk, Barbara Wilson, James F Lauc, Gordan |
| Author_xml | – sequence: 1 givenname: Maja surname: Pucić fullname: Pucić, Maja organization: Genos Ltd., Glycobiology Division, Planinska 1, 10000 Zagreb, Croatia – sequence: 2 givenname: Ana surname: Knezević fullname: Knezević, Ana – sequence: 3 givenname: Jana surname: Vidic fullname: Vidic, Jana – sequence: 4 givenname: Barbara surname: Adamczyk fullname: Adamczyk, Barbara – sequence: 5 givenname: Mislav surname: Novokmet fullname: Novokmet, Mislav – sequence: 6 givenname: Ozren surname: Polasek fullname: Polasek, Ozren – sequence: 7 givenname: Olga surname: Gornik fullname: Gornik, Olga – sequence: 8 givenname: Sandra surname: Supraha-Goreta fullname: Supraha-Goreta, Sandra – sequence: 9 givenname: Mark R surname: Wormald fullname: Wormald, Mark R – sequence: 10 givenname: Irma surname: Redzić fullname: Redzić, Irma – sequence: 11 givenname: Harry surname: Campbell fullname: Campbell, Harry – sequence: 12 givenname: Alan surname: Wright fullname: Wright, Alan – sequence: 13 givenname: Nicholas D surname: Hastie fullname: Hastie, Nicholas D – sequence: 14 givenname: James F surname: Wilson fullname: Wilson, James F – sequence: 15 givenname: Igor surname: Rudan fullname: Rudan, Igor – sequence: 16 givenname: Manfred surname: Wuhrer fullname: Wuhrer, Manfred – sequence: 17 givenname: Pauline M surname: Rudd fullname: Rudd, Pauline M – sequence: 18 givenname: Djuro surname: Josić fullname: Josić, Djuro – sequence: 19 givenname: Gordan surname: Lauc fullname: Lauc, Gordan |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/21653738$$D View this record in MEDLINE/PubMed |
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| PublicationTitle | Molecular & cellular proteomics |
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| Snippet | All immunoglobulin G molecules carry N-glycans, which modulate their biological activity. Changes in N-glycosylation of IgG associate with various diseases and... |
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| SubjectTerms | Adolescent Adult Aged Aged, 80 and over Female Fucose - metabolism Genetic Variation Glycomics - methods Glycoproteins - chemistry Glycoproteins - genetics Glycoproteins - isolation & purification Glycosylation High-Throughput Screening Assays Humans Immunoglobulin G - chemistry Immunoglobulin G - genetics Immunoglobulin G - isolation & purification Male Middle Aged Models, Molecular ortho-Aminobenzoates - chemistry Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase - chemistry Polysaccharides - chemistry Population |
| Title | High throughput isolation and glycosylation analysis of IgG-variability and heritability of the IgG glycome in three isolated human populations |
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