ArticleNature chemical biology2021
Yeast- and antibody-based tools for studying tryptophan C-mannosylation.
Article in Nature chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- The biology of interleukin-6 family cytokines is regulated by glycosylation.The Biochemical journal · 2025Review
- Methods for detecting, building, and improving tryptophan mannosylation in glycoprotein structures.Protein science : a publication of the Protein Society · 2025Article
- Implications of glycosylation for the development of selected cytokines and their derivatives for medical use.Biotechnology advances · 2024Review
- Global View of Domain-Specific O-Linked Mannose Glycosylation in Glycoengineered Cells.Molecular & cellular proteomics : MCP · 2024Article
- Article
- Recent trends in glycoproteomics by characterization of intact glycopeptides.Analytical and bioanalytical chemistry · 2023Review
- Deciphering the Properties and Functions of Glycoproteins Using Quantitative Proteomics.Journal of proteome research · 2023Review
- Anti-glycan monoclonal antibodies: Basic research and clinical applications.Current opinion in chemical biology · 2023Review
- Structure, sequon recognition and mechanism of tryptophan C-mannosyltransferase.Nature chemical biology · 2023Article
- Conservation, abundance, glycosylation profile, and localization of the TSP protein family in Cryptosporidium parvum.The Journal of biological chemistry · 2023Article
- Tryptophan C-mannosylation is critical for Plasmodium falciparum transmission.Nature communications · 2022Article
- ProteinMolecules (Basel, Switzerland) · 2021Review
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tryptophan C-mannosylation is an unusual co-translational protein modification performed by metazoans and apicomplexan protists. The prevalence and biological functions of this modification are poorly understood, with progress in the field hampered by a dearth of convenient tools for installing and detecting the modification. Here, we engineer a yeast system to produce a diverse array of proteins with and without tryptophan C-mannosylation and interrogate the modification's influence on protein stability and function. This system also enabled mutagenesis studies to identify residues of the glycosyltransferase and its protein substrates that are crucial for catalysis. The collection of modified proteins accrued during this work facilitated the generation and thorough characterization of monoclonal antibodies against tryptophan C-mannosylation. These antibodies empowered proteomic analyses of the brain C-glycome by enriching for peptides possessing tryptophan C-mannosylation. This study revealed many new modification sites on proteins throughout the secretory pathway with both conventional and non-canonical consensus sequences.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.