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Article ; Online: Chemical tools to track and perturb the expression of sialic acid and fucose monosaccharides.

Rossing, Emiel / Pijnenborg, Johan F A / Boltje, Thomas J

Chemical communications (Cambridge, England)

2022 Volume 58, Issue 87, Page(s) 12139–12150

Abstract: The biosynthesis of glycans is a highly conserved biological process and found in all domains of life. The expression of cell surface glycans is increasingly recognized as a target for therapeutic intervention given the role of glycans in major ... ...

Abstract	The biosynthesis of glycans is a highly conserved biological process and found in all domains of life. The expression of cell surface glycans is increasingly recognized as a target for therapeutic intervention given the role of glycans in major pathologies such as cancer and microbial infection. Herein, we summarize our contributions to the development of unnatural monosaccharide derivatives to infiltrate and alter the expression of both mammalian and bacterial glycans and their therapeutic application.
MeSH term(s)	Animals ; Fucose/chemistry ; Mammals ; Monosaccharides/chemistry ; N-Acetylneuraminic Acid/chemistry ; Polysaccharides/biosynthesis ; Polysaccharides/chemistry ; Bacteria
Chemical Substances	Fucose (28RYY2IV3F) ; Monosaccharides ; N-Acetylneuraminic Acid (GZP2782OP0) ; Polysaccharides
Language	English
Publishing date	2022-11-01
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1472881-3
ISSN	1364-548X ; 1359-7345 ; 0009-241X
ISSN (online)	1364-548X
ISSN	1359-7345 ; 0009-241X
DOI	10.1039/d2cc04275d
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Article ; Online: Structure-Activity Relationship of Metabolic Sialic Acid Inhibitors and Labeling Reagents.

Moons, Sam J / Rossing, Emiel / Janssen, Mathilde A C H / Heise, Torben / Büll, Christian / Adema, Gosse J / Boltje, Thomas J

ACS chemical biology

2022 Volume 17, Issue 3, Page(s) 590–597

Abstract: Sialic acids cap the glycans of cell surface glycoproteins and glycolipids. They are involved in a multitude of biological processes, and aberrant sialic acid expression is associated with several pathologies, such as cancer. Strategies to interfere with ...

Abstract	Sialic acids cap the glycans of cell surface glycoproteins and glycolipids. They are involved in a multitude of biological processes, and aberrant sialic acid expression is associated with several pathologies, such as cancer. Strategies to interfere with the sialic acid biosynthesis can potentially be used for anticancer therapy. One well-known class of sialylation inhibitors is peracetylated 3-fluorosialic acids. We synthesized 3-fluorosialic acid derivatives modified at the C-4, C-5, C-8, and C-9 position and tested their inhibitory potency in vitro. Modifications at C-5 lead to increased inhibition, compared to the natural acetamide at this position. These structure-activity relationships could also be applied to improve the efficiency of sialic acid metabolic labeling reagents by modification of the C-5 position. Hence, these results improve our understanding of the structure-activity relationships of sialic acid glycomimetics and their metabolic processing.
MeSH term(s)	Indicators and Reagents ; N-Acetylneuraminic Acid/metabolism ; Polysaccharides/metabolism ; Sialic Acids/metabolism ; Structure-Activity Relationship
Chemical Substances	Indicators and Reagents ; Polysaccharides ; Sialic Acids ; N-Acetylneuraminic Acid (GZP2782OP0)
Language	English
Publishing date	2022-02-18
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1554-8937
ISSN (online)	1554-8937
DOI	10.1021/acschembio.1c00868
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Article ; Online: Cellular Fucosylation Inhibitors Based on Fluorinated Fucose-1-phosphates*.

Pijnenborg, Johan F A / Visser, Eline A / Noga, Marek / Rossing, Emiel / Veizaj, Raisa / Lefeber, Dirk J / Büll, Christian / Boltje, Thomas J

Chemistry (Weinheim an der Bergstrasse, Germany)

2021 Volume 27, Issue 12, Page(s) 4022–4027

Abstract: Fucosylation of glycans impacts a myriad of physiological and pathological processes. Inhibition of fucose expression emerges as a potential therapeutic avenue for example in cancer, inflammation, and infection. In this study, we found that protected 2- ... ...

Abstract	Fucosylation of glycans impacts a myriad of physiological and pathological processes. Inhibition of fucose expression emerges as a potential therapeutic avenue for example in cancer, inflammation, and infection. In this study, we found that protected 2-fluorofucose 1-phosphate efficiently inhibits cellular fucosylation with a four to seven times higher potency than known inhibitor 2FF, independently of the anomeric stereochemistry. Nucleotide sugar analysis revealed that both the α- and β-GDP-2FF anomers are formed inside the cell. In conclusion, we developed A2FF1P and B2FF1P as potent new tools for studying the role of fucosylation in health and disease and they are potential therapeutic candidates.
MeSH term(s)	Cell Line, Tumor ; Fucose ; Glycosylation ; Phosphates ; Polysaccharides
Chemical Substances	Phosphates ; Polysaccharides ; Fucose (28RYY2IV3F)
Language	English
Publishing date	2021-02-02
Publishing country	Germany
Document type	Journal Article
ZDB-ID	1478547-X
ISSN	1521-3765 ; 0947-6539
ISSN (online)	1521-3765
ISSN	0947-6539
DOI	10.1002/chem.202005359
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Article ; Online: Two Receptor Binding Strategy of SARS-CoV-2 Is Mediated by Both the N-Terminal and Receptor-Binding Spike Domain.

Monti, Michele / Milanetti, Edoardo / Frans, Myrthe T / Miotto, Mattia / Di Rienzo, Lorenzo / Baranov, Maksim V / Gosti, Giorgio / Somavarapu, Arun Kumar / Nagaraj, Madhu / Golbek, Thaddeus W / Rossing, Emiel / Moons, Sam J / Boltje, Thomas J / van den Bogaart, Geert / Weidner, Tobias / Otzen, Daniel E / Tartaglia, Gian Gaetano / Ruocco, Giancarlo / Roeters, Steven J

The journal of physical chemistry. B

2024 Volume 128, Issue 2, Page(s) 451–464

Abstract: It is not well understood why severe acute respiratory syndrome (SARS)-CoV-2 spreads much faster than other β-coronaviruses such as SARS-CoV and Middle East respiratory syndrome (MERS)-CoV. In a previous publication, we predicted the binding of the N- ... ...

Abstract	It is not well understood why severe acute respiratory syndrome (SARS)-CoV-2 spreads much faster than other β-coronaviruses such as SARS-CoV and Middle East respiratory syndrome (MERS)-CoV. In a previous publication, we predicted the binding of the N-terminal domain (NTD) of SARS-CoV-2 spike to sialic acids (SAs). Here, we experimentally validate this interaction and present simulations that reveal a second possible interaction between SAs and the spike protein via a binding site located in the receptor-binding domain (RBD). The predictions from molecular-dynamics simulations and the previously-published 2D-Zernike binding-site recognition approach were validated through flow-induced dispersion analysis (FIDA)─which reveals the capability of the SARS-CoV-2 spike to bind to SA-containing (glyco)lipid vesicles, and flow-cytometry measurements─which show that spike binding is strongly decreased upon inhibition of SA expression on the membranes of angiotensin converting enzyme-2 (ACE2)-expressing HEK cells. Our analyses reveal that the SA binding of the NTD and RBD strongly enhances the infection-inducing ACE2 binding. Altogether, our work provides
MeSH term(s)	Humans ; SARS-CoV-2 ; Angiotensin-Converting Enzyme 2 ; COVID-19 ; Protein Binding ; Binding Sites
Chemical Substances	Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
Language	English
Publishing date	2024-01-08
Publishing country	United States
Document type	Journal Article
ISSN	1520-5207
ISSN (online)	1520-5207
DOI	10.1021/acs.jpcb.3c06258
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Article ; Online: Targeting aberrant sialylation and fucosylation in prostate cancer cells using potent metabolic inhibitors.

Orozco-Moreno, Margarita / Visser, Eline A / Hodgson, Kirsty / Hipgrave Ederveen, Agnes L / Bastian, Kayla / Goode, Emily Archer / Öztürk, Özden / Pijnenborg, Johan F A / Eerden, Nienke / Moons, Sam J / Rossing, Emiel / Wang, Ning / de Haan, Noortje / Büll, Christian / Boltje, Thomas J / Munkley, Jennifer

Glycobiology

2023 Volume 33, Issue 12, Page(s) 1155–1171

Abstract: Aberrant glycosylation is a hallmark of cancer and is not just a consequence, but also a driver of a malignant phenotype. In prostate cancer, changes in fucosylated and sialylated glycans are common and this has important implications for tumor ... ...

Abstract	Aberrant glycosylation is a hallmark of cancer and is not just a consequence, but also a driver of a malignant phenotype. In prostate cancer, changes in fucosylated and sialylated glycans are common and this has important implications for tumor progression, metastasis, and immune evasion. Glycans hold huge translational potential and new therapies targeting tumor-associated glycans are currently being tested in clinical trials for several tumor types. Inhibitors targeting fucosylation and sialylation have been developed and show promise for cancer treatment, but translational development is hampered by safety issues related to systemic adverse effects. Recently, potent metabolic inhibitors of sialylation and fucosylation were designed that reach higher effective concentrations within the cell, thereby rendering them useful tools to study sialylation and fucosylation as potential candidates for therapeutic testing. Here, we investigated the effects of global metabolic inhibitors of fucosylation and sialylation in the context of prostate cancer progression. We find that these inhibitors effectively shut down the synthesis of sialylated and fucosylated glycans to remodel the prostate cancer glycome with only minor apparent side effects on other glycan types. Our results demonstrate that treatment with inhibitors targeting fucosylation or sialylation decreases prostate cancer cell growth and downregulates the expression of genes and proteins important in the trajectory of disease progression. We anticipate our findings will lead to the broader use of metabolic inhibitors to explore the role of fucosylated and sialylated glycans in prostate tumor pathology and may pave the way for the development of new therapies for prostate cancer.
MeSH term(s)	Male ; Humans ; Glycosylation ; Prostatic Neoplasms/drug therapy ; Prostatic Neoplasms/metabolism ; Protein Processing, Post-Translational ; Polysaccharides/metabolism
Chemical Substances	Polysaccharides
Language	English
Publishing date	2023-10-17
Publishing country	England
Document type	Journal Article
ZDB-ID	1067689-2
ISSN	1460-2423 ; 0959-6658
ISSN (online)	1460-2423
ISSN	0959-6658
DOI	10.1093/glycob/cwad085
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Article ; Online: Luminescent Assay for the Screening of SARS-CoV-2 M

Sondag, Daan / Merx, Jona / Rossing, Emiel / Boltje, Thomas J / Löwik, Dennis W P M / Nelissen, Frank H T / van Geffen, Mark / van 't Veer, Cornelis / van Heerde, Waander L / Rutjes, Floris P J T

Chembiochem : a European journal of chemical biology

2022 Volume 23, Issue 15, Page(s) e202200190

Abstract: Since the outbreak of SARS-CoV-2 in December 2019 millions of infections have been reported globally. The viral chymotrypsin-like main protease ( ... ...

Abstract	Since the outbreak of SARS-CoV-2 in December 2019 millions of infections have been reported globally. The viral chymotrypsin-like main protease (M
MeSH term(s)	Antiviral Agents/pharmacology ; COVID-19/drug therapy ; Coronavirus 3C Proteases ; Cysteine Endopeptidases ; Humans ; Luminescent Measurements ; Molecular Docking Simulation ; Protease Inhibitors/pharmacology ; SARS-CoV-2 ; Viral Nonstructural Proteins
Chemical Substances	Antiviral Agents ; Protease Inhibitors ; Viral Nonstructural Proteins ; Cysteine Endopeptidases (EC 3.4.22.-) ; Coronavirus 3C Proteases (EC 3.4.22.28)
Language	English
Publishing date	2022-06-14
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2020469-3
ISSN	1439-7633 ; 1439-4227
ISSN (online)	1439-7633
ISSN	1439-4227
DOI	10.1002/cbic.202200190
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Article ; Online: Modular synthesis and immunological evaluation of suspected allergenic galactooligosaccharides.

Elferink, Hidde / Rossing, Emiel / Huang, Chiung-Hui / Lee, Bee Wah / Cao, Linqiu / Delsing, Dianne J / Groeneveld, Andre / Boltje, Thomas J

Organic & biomolecular chemistry

2019 Volume 17, Issue 12, Page(s) 3108–3112

Abstract: Galactooligosaccharides (GOS) are widely used in the food industry as prebiotics and in very rare cases, can lead to an allergic reaction. Due to the microheterogeneity of GOS it is very difficult to extract pure and well defined oligosaccharides to ... ...

Abstract	Galactooligosaccharides (GOS) are widely used in the food industry as prebiotics and in very rare cases, can lead to an allergic reaction. Due to the microheterogeneity of GOS it is very difficult to extract pure and well defined oligosaccharides to establish which component is responsible for the observed allergenicity. Herein, we report the chemical synthesis of a suspected allergen 4PX and three closely related oligosaccharides based on a modular approach. The fact that synthesized 4PX and a regioisomer did not cause basophil activation in subjects with confirmed GOS-allergy excludes both tetrasaccharides as key-epitopes in GOS-allergenicity in Singapore.
Language	English
Publishing date	2019-04-02
Publishing country	England
Document type	Journal Article
ZDB-ID	2097583-1
ISSN	1477-0539 ; 1477-0520
ISSN (online)	1477-0539
ISSN	1477-0520
DOI	10.1039/c9ob00108e
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Article ; Online: Fluorinated rhamnosides inhibit cellular fucosylation.

Pijnenborg, Johan F A / Rossing, Emiel / Merx, Jona / Noga, Marek J / Titulaer, Willem H C / Eerden, Nienke / Veizaj, Raisa / White, Paul B / Lefeber, Dirk J / Boltje, Thomas J

Nature communications

2021 Volume 12, Issue 1, Page(s) 7024

Abstract: The sugar fucose is expressed on mammalian cell membranes as part of glycoconjugates and mediates essential physiological processes. The aberrant expression of fucosylated glycans has been linked to pathologies such as cancer, inflammation, infection, ... ...

Abstract	The sugar fucose is expressed on mammalian cell membranes as part of glycoconjugates and mediates essential physiological processes. The aberrant expression of fucosylated glycans has been linked to pathologies such as cancer, inflammation, infection, and genetic disorders. Tools to modulate fucose expression on living cells are needed to elucidate the biological role of fucose sugars and the development of potential therapeutics. Herein, we report a class of fucosylation inhibitors directly targeting de novo GDP-fucose biosynthesis via competitive GMDS inhibition. We demonstrate that cell permeable fluorinated rhamnose 1-phosphate derivatives (Fucotrim I & II) are metabolic prodrugs that are metabolized to their respective GDP-mannose derivatives and efficiently inhibit cellular fucosylation.
MeSH term(s)	Animals ; Carbohydrate Sequence ; Cell Line, Tumor ; Cell Membrane/drug effects ; Drug Design ; Enzyme Inhibitors/chemical synthesis ; Enzyme Inhibitors/pharmacology ; Fucose/chemistry ; Gene Expression ; Glycosylation/drug effects ; Guanosine Diphosphate Fucose/antagonists & inhibitors ; Guanosine Diphosphate Fucose/biosynthesis ; Halogenation ; Humans ; Hydro-Lyases/antagonists & inhibitors ; Hydro-Lyases/genetics ; Hydro-Lyases/metabolism ; Jurkat Cells ; Lymphocytes/cytology ; Lymphocytes/drug effects ; Lymphocytes/metabolism ; Mice ; Prodrugs/chemical synthesis ; Prodrugs/pharmacology ; Structure-Activity Relationship ; THP-1 Cells
Chemical Substances	Enzyme Inhibitors ; Prodrugs ; Guanosine Diphosphate Fucose (15839-70-0) ; Fucose (28RYY2IV3F) ; Hydro-Lyases (EC 4.2.1.-) ; GDPmannose 4,6-dehydratase (EC 4.2.1.47)
Language	English
Publishing date	2021-12-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-021-27355-9
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Article ; Online: Structure-Activity Relationship of Fluorinated Sialic Acid Inhibitors for Bacterial Sialylation.

Moons, Sam J / Rossing, Emiel / Heming, Jurriaan J A / Janssen, Mathilde A C H / van Scherpenzeel, Monique / Lefeber, Dirk J / de Jonge, Marien I / Langereis, Jeroen D / Boltje, Thomas J

Bioconjugate chemistry

2021 Volume 32, Issue 6, Page(s) 1047–1051

Abstract: Bacterial pathogens such as ... ...

Abstract	Bacterial pathogens such as Nontypeable
MeSH term(s)	Haemophilus influenzae/drug effects ; Haemophilus influenzae/metabolism ; Halogenation ; N-Acetylneuraminic Acid/chemistry ; N-Acetylneuraminic Acid/pharmacology ; Structure-Activity Relationship
Chemical Substances	N-Acetylneuraminic Acid (GZP2782OP0)
Language	English
Publishing date	2021-05-27
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1024041-x
ISSN	1520-4812 ; 1043-1802
ISSN (online)	1520-4812
ISSN	1043-1802
DOI	10.1021/acs.bioconjchem.1c00194
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Article ; Online: Selective Inhibition of Sialic Acid-Based Molecular Mimicry in Haemophilus influenzae Abrogates Serum Resistance.

Heise, Torben / Langereis, Jeroen D / Rossing, Emiel / de Jonge, Marien I / Adema, Gosse J / Büll, Christian / Boltje, Thomas J

Cell chemical biology

2018 Volume 25, Issue 10, Page(s) 1279–1285.e8

Abstract: Pathogens such as non-typeable Haemophilus influenzae (NTHi) evade the immune system by presenting host-derived sialic acids. NTHi cannot synthesize sialic acids and therefore needs to utilize sialic acids originating from host tissue. Here we report ... ...

Abstract	Pathogens such as non-typeable Haemophilus influenzae (NTHi) evade the immune system by presenting host-derived sialic acids. NTHi cannot synthesize sialic acids and therefore needs to utilize sialic acids originating from host tissue. Here we report sialic acid-based probes to visualize and inhibit the transfer of host sialic acids to NTHi. Inhibition of sialic acid utilization by NTHi enhanced serum-mediated killing. Furthermore, in an in vitro model of the human respiratory tract, we demonstrate efficient inhibition of sialic acid transfer from primary human bronchial epithelial cells to NTHi using bioorthogonal chemistry.
MeSH term(s)	Antiviral Agents/chemistry ; Antiviral Agents/pharmacology ; Cell Line ; Cells, Cultured ; Haemophilus Infections/blood ; Haemophilus Infections/drug therapy ; Haemophilus Infections/metabolism ; Haemophilus influenzae/drug effects ; Haemophilus influenzae/metabolism ; Humans ; N-Acetylneuraminic Acid/analogs & derivatives ; N-Acetylneuraminic Acid/metabolism ; N-Acetylneuraminic Acid/pharmacology ; Respiratory Mucosa/cytology ; Respiratory Mucosa/drug effects ; Respiratory Mucosa/metabolism ; Respiratory Mucosa/virology ; Sialyltransferases/antagonists & inhibitors ; Sialyltransferases/metabolism
Chemical Substances	Antiviral Agents ; Sialyltransferases (EC 2.4.99.-) ; N-Acetylneuraminic Acid (GZP2782OP0)
Language	English
Publishing date	2018-07-05
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2451-9448
ISSN (online)	2451-9448
DOI	10.1016/j.chembiol.2018.05.018
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