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7 results on '"Koeleman, Carolien A. M."'

1. IgG Fab Glycans Hinder FcRn-Mediated Placental Transport

Author

Sub Biomol.Mass Spectrometry & Proteom., Afd Biomol.Mass Spect. and Proteomics, Biomolecular Mass Spectrometry and Proteomics, Volkov, Mikhail, Brinkhaus, Maximilian, van Schie, Karin A, Bondt, Albert, Kissel, Theresa, van der Kooi, Elvera J, Bentlage, Arthur E H, Koeleman, Carolien A M, de Taeye, Steven W, Derksen, Ninotska I, Dolhain, Radboud J E M, Braig-Scherer, Ute, Huizinga, Tom W J, Wuhrer, Manfred, Toes, René E M, Vidarsson, Gestur, van der Woude, Diane, Sub Biomol.Mass Spectrometry & Proteom., Afd Biomol.Mass Spect. and Proteomics, Biomolecular Mass Spectrometry and Proteomics, Volkov, Mikhail, Brinkhaus, Maximilian, van Schie, Karin A, Bondt, Albert, Kissel, Theresa, van der Kooi, Elvera J, Bentlage, Arthur E H, Koeleman, Carolien A M, de Taeye, Steven W, Derksen, Ninotska I, Dolhain, Radboud J E M, Braig-Scherer, Ute, Huizinga, Tom W J, Wuhrer, Manfred, Toes, René E M, Vidarsson, Gestur, and van der Woude, Diane

Published
2023

2. IgG Fab Glycans Hinder FcRn-Mediated Placental Transport

Author

Sub Biomol.Mass Spectrometry & Proteom., Afd Biomol.Mass Spect. and Proteomics, Biomolecular Mass Spectrometry and Proteomics, Volkov, Mikhail, Brinkhaus, Maximilian, van Schie, Karin A, Bondt, Albert, Kissel, Theresa, van der Kooi, Elvera J, Bentlage, Arthur E H, Koeleman, Carolien A M, de Taeye, Steven W, Derksen, Ninotska I, Dolhain, Radboud J E M, Braig-Scherer, Ute, Huizinga, Tom W J, Wuhrer, Manfred, Toes, René E M, Vidarsson, Gestur, van der Woude, Diane, Sub Biomol.Mass Spectrometry & Proteom., Afd Biomol.Mass Spect. and Proteomics, Biomolecular Mass Spectrometry and Proteomics, Volkov, Mikhail, Brinkhaus, Maximilian, van Schie, Karin A, Bondt, Albert, Kissel, Theresa, van der Kooi, Elvera J, Bentlage, Arthur E H, Koeleman, Carolien A M, de Taeye, Steven W, Derksen, Ninotska I, Dolhain, Radboud J E M, Braig-Scherer, Ute, Huizinga, Tom W J, Wuhrer, Manfred, Toes, René E M, Vidarsson, Gestur, and van der Woude, Diane

Published
2023

3. Afucosylated Plasmodium falciparum-specific IgG is induced by infection but not by subunit vaccination

Author

Larsen, Mads Delbo, Lopez-Perez, Mary, Dickson, Emmanuel Kakra, Ampomah, Paulina, Tuikue Ndam, Nicaise, Nouta, Jan, Koeleman, Carolien A M, Ederveen, Agnes L Hipgrave, Mordmüller, Benjamin, Salanti, Ali, Nielsen, Morten Agertoug, Massougbodji, Achille, van der Schoot, C Ellen, Ofori, Michael F, Wuhrer, Manfred, Hviid, Lars, Vidarsson, Gestur, Larsen, Mads Delbo, Lopez-Perez, Mary, Dickson, Emmanuel Kakra, Ampomah, Paulina, Tuikue Ndam, Nicaise, Nouta, Jan, Koeleman, Carolien A M, Ederveen, Agnes L Hipgrave, Mordmüller, Benjamin, Salanti, Ali, Nielsen, Morten Agertoug, Massougbodji, Achille, van der Schoot, C Ellen, Ofori, Michael F, Wuhrer, Manfred, Hviid, Lars, and Vidarsson, Gestur

Abstract

Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) family members mediate receptor- and tissue-specific sequestration of infected erythrocytes (IEs) in malaria. Antibody responses are a central component of naturally acquired malaria immunity. PfEMP1-specific IgG likely protects by inhibiting IE sequestration and through IgG-Fc Receptor (FcγR) mediated phagocytosis and killing of antibody-opsonized IEs. The affinity of afucosylated IgG to FcγRIIIa is up to 40-fold higher than fucosylated IgG, resulting in enhanced antibody-dependent cellular cytotoxicity. Most IgG in plasma is fully fucosylated, but afucosylated IgG is elicited in response to enveloped viruses and to paternal alloantigens during pregnancy. Here we show that naturally acquired PfEMP1-specific IgG is strongly afucosylated in a stable and exposure-dependent manner, and efficiently induces FcγRIIIa-dependent natural killer (NK) cell degranulation. In contrast, immunization with a subunit PfEMP1 (VAR2CSA) vaccine results in fully fucosylated specific IgG. These results have implications for understanding protective natural- and vaccine-induced immunity to malaria.

Published
2021

4. Simultaneous Immunoglobulin A and G Glycopeptide Profiling for High-Throughput Applications

Author

Momčilović, Ana, de Haan, Noortje, Hipgrave Ederveen, Agnes L, Bondt, Albert, Koeleman, Carolien A M, Falck, David, de Neef, Louise A, Mesker, Wilma E, Tollenaar, Rob, de Ru, Arnoud, van Veelen, Peter, Wuhrer, Manfred, Dotz, Viktoria, Momčilović, Ana, de Haan, Noortje, Hipgrave Ederveen, Agnes L, Bondt, Albert, Koeleman, Carolien A M, Falck, David, de Neef, Louise A, Mesker, Wilma E, Tollenaar, Rob, de Ru, Arnoud, van Veelen, Peter, Wuhrer, Manfred, and Dotz, Viktoria

Published
2020

5. Simultaneous Immunoglobulin A and G Glycopeptide Profiling for High-Throughput Applications

Author

Momčilović, Ana, de Haan, Noortje, Hipgrave Ederveen, Agnes L, Bondt, Albert, Koeleman, Carolien A M, Falck, David, de Neef, Louise A, Mesker, Wilma E, Tollenaar, Rob, de Ru, Arnoud, van Veelen, Peter, Wuhrer, Manfred, Dotz, Viktoria, Momčilović, Ana, de Haan, Noortje, Hipgrave Ederveen, Agnes L, Bondt, Albert, Koeleman, Carolien A M, Falck, David, de Neef, Louise A, Mesker, Wilma E, Tollenaar, Rob, de Ru, Arnoud, van Veelen, Peter, Wuhrer, Manfred, and Dotz, Viktoria

Published
2020

6. Simultaneous Immunoglobulin A and G Glycopeptide Profiling for High-Throughput Applications

Author

Momčilović, Ana, de Haan, Noortje, Hipgrave Ederveen, Agnes L, Bondt, Albert, Koeleman, Carolien A M, Falck, David, de Neef, Louise A, Mesker, Wilma E, Tollenaar, Rob, de Ru, Arnoud, van Veelen, Peter, Wuhrer, Manfred, Dotz, Viktoria, Momčilović, Ana, de Haan, Noortje, Hipgrave Ederveen, Agnes L, Bondt, Albert, Koeleman, Carolien A M, Falck, David, de Neef, Louise A, Mesker, Wilma E, Tollenaar, Rob, de Ru, Arnoud, van Veelen, Peter, Wuhrer, Manfred, and Dotz, Viktoria

Published
2020

7. Polymorphisms in B3GAT1, SLC9A9 and MGAT5 are associated with variation within the human plasma N-glycome of 3533 European adults

Author

Huffman, Jennifer E., Knezevic, Ana, Vitart, Veronique, Kattla, Jayesh, Adamczyk, Barbara, Novokmet, Mislav, Igl, Wilmar, Pucic, Maja, Zgaga, Lina, Johansson, Åsa, Redzic, Irma, Gornik, Olga, Zemunik, Tatijana, Polasek, Ozren, Kolcic, Ivana, Pehlic, Marina, Koeleman, Carolien A. M., Campbell, Susan, Wild, Sarah H., Hastie, Nicholas D., Campbell, Harry, Gyllensten, Ulf, Wuhrer, Manfred, Wilson, James F., Hayward, Caroline, Rudan, Igor, Rudd, Pauline M., Wright, Alan F., Lauc, Gordan, Huffman, Jennifer E., Knezevic, Ana, Vitart, Veronique, Kattla, Jayesh, Adamczyk, Barbara, Novokmet, Mislav, Igl, Wilmar, Pucic, Maja, Zgaga, Lina, Johansson, Åsa, Redzic, Irma, Gornik, Olga, Zemunik, Tatijana, Polasek, Ozren, Kolcic, Ivana, Pehlic, Marina, Koeleman, Carolien A. M., Campbell, Susan, Wild, Sarah H., Hastie, Nicholas D., Campbell, Harry, Gyllensten, Ulf, Wuhrer, Manfred, Wilson, James F., Hayward, Caroline, Rudan, Igor, Rudd, Pauline M., Wright, Alan F., and Lauc, Gordan

Abstract

The majority of human proteins are post-translationally modified by covalent addition of one or more complex oligosaccharides (glycans). Alterations in glycosylation processing are associated with numerous diseases and glycans are attracting increasing attention both as disease biomarkers and as targets for novel therapeutic approaches. Using a recently developed high-throughput high-performance liquid chromatography (HPLC) analysis method, we have reported, in a pilot genome-wide association study of 13 glycan features in 2705 individuals from three European populations, that polymorphisms at three loci (FUT8, FUT6/FUT3 and HNF1A) affect plasma levels of N-glycans. Here, we extended the analysis to 33 directly measured and 13 derived glycosylation traits in 3533 individuals and identified three novel gene association (MGAT5, B3GAT1 and SLC9A9) as well as replicated the previous findings using an additional European cohort. MGAT5 (meta-analysis association P-value = 1.80 x 10(-10) for rs1257220) encodes a glycosyltransferase which is known to synthesize the associated glycans. In contrast, neither B3GAT1 (rs7928758, P = 1.66 x 10(-08)) nor SLC9A9 (rs4839604, P = 3.50 x 10(-13)) had previously been associated functionally with glycosylation of plasma proteins. Given the glucuronyl transferase activity of B3GAT1, we were able to show that glucuronic acid is present on antennae of plasma glycoproteins underlying the corresponding HPLC peak. SLC9A9 encodes a proton pump which affects pH in the endosomal compartment and it was recently reported that changes in Golgi pH can impair protein sialylation, giving a possible mechanism for the observed association.

Published
2011
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