Anomalies congénitales de la glycosylation (CDG)

Houdou, Marine; Foulquier, François

doi:10.1051/medsci/2020128

Cited by 2 publications

(1 citation statement)

References 56 publications

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“…The discovery of TMEM165 as a gene related to human CDG (Houdou & Foulquier, 2020 ) began a new era in the understanding of the regulation of Golgi Mn 2+ homeostasis (Foulquier et al ., 2012 ). An understanding of the crucial role of TMEM165 in Golgi glycosylation maintenance arose unambiguously from the identification of CDG patients with mutations in TMEM165 .…”

Section: Regulation Of the N ‐Glycosylation Pa...mentioning

confidence: 99%

Towards understanding the extensive diversity of protein N‐glycan structures in eukaryotes

et al. 2021

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N‐glycosylation is an important post‐translational modification of proteins that has been highly conserved during evolution and is found in Eukaryota, Bacteria and Archaea. In eukaryotes, N‐glycan processing is sequential, involving multiple specific steps within the secretory pathway as proteins travel through the endoplasmic reticulum and the Golgi apparatus. In this review, we first summarize the different steps of the N‐glycan processing and further describe recent findings regarding the diversity of N‐glycan structures in eukaryotic clades. This comparison allows us to explore the different regulation mechanisms of N‐glycan processing among eukaryotic clades. Recent findings regarding the regulation of protein N‐glycosylation are highlighted, especially the regulation of the biosynthesis of complex‐type N‐glycans through manganese and calcium homeostasis and the specific role of transmembrane protein 165 (TMEM165) for which homologous sequences have been identified in several eukaryotic clades. Further research will be required to characterize the function of TMEM165 homologous sequences in different eukaryotic clades.

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Section: Regulation Of the N ‐Glycosylation Pa...mentioning

confidence: 99%

Towards understanding the extensive diversity of protein N‐glycan structures in eukaryotes

et al. 2021

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Minimal epitope for Mannitou IgM on paucimannose-carrying glycoproteins

et al. 2021

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Paucimannosidic glycans are restricted to the core structure [Man1–3GlcNAc2Fuc0–1] of N-glycans and are rarely found in mammalian tissues. Yet, especially [Man2-3GlcNAc2Fuc1] have been found significantly upregulated in tumors, including in colorectal and liver cancer. Mannitou IgM is a murine monoclonal antibody that was previously shown to recognise Man3GlcNAc2 with an almost exclusive selectivity. Here, we have sought the definition of the minimal glycan epitope of Mannitou IgM, initiated by screening on a newly designed paucimannosidic glycan microarray. Among the best binders were Man3GlcNAc2 and its α1,6 core-fucosylated variant, Man3GlcNAc2Fuc1. Unexpectedly and in contrast to earlier findings, Man5GlcNAc2-type structures bind equally well and a large tolerance was observed for substitutions on the α1,6 arm. It was confirmed that any substitution on the single α1,3-linked mannose completely abolishes binding. Surface plasmon resonance for kinetic measurements of Mannitou IgM binding, either directly on the glycans or as presented on omega-1 and kappa-5 soluble egg antigens from the helminth parasite Schistosoma mansoni, showed submicromolar affinities. To characterize the epitope in greater and atomic detail, saturation transfer difference nuclear magnetic resonance spectroscopy was performed with the Mannitou antigen-binding fragment. The STD-NMR data demonstrated the strongest interactions with the aliphatic protons H1 and H2 of the α1–3-linked mannose, and weaker imprints on its H3, H4 and H5 protons. In conclusion, Mannitou IgM binding requires a non-substituted α1,3-linked mannose branch of paucimannose also on proteins, making it a highly specific tool for the distinction of concurrent human tumor-associated carbohydrate antigens.

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Anomalies congénitales de la glycosylation (CDG)

Cited by 2 publications

References 56 publications

Towards understanding the extensive diversity of protein N‐glycan structures in eukaryotes

Towards understanding the extensive diversity of protein N‐glycan structures in eukaryotes

Minimal epitope for Mannitou IgM on paucimannose-carrying glycoproteins

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