Current strategies for characterization of mucin-domain glycoproteins
Abstract
Glycosylation, and especially O-linked glycosylation, remains a critical blind spot in the understanding of post-translational modifications. Due to their nature as proteins defined by a large density and abundance of O-glycosylation, mucins present extra challenges in the analysis of their structure and function. However, recent breakthroughs in multiple areas of research have rendered mucin-domain glycoproteins more accessible to current characterization techniques. In particular, the adaptation of mucinases to glycoproteomic workflows, the manipulation of cellular glycosylation pathways, and the advances in synthetic methods to more closely mimic mucin domains have introduced new and exciting avenues to study mucin glycoproteins. Here, we summarize recent developments in understanding the structure and biological function of mucin domains and their associated glycans, from glycoproteomic tools and visualization methods to synthetic glycopeptide mimetics.
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Mucin-type glycosylation can regulate various cellular functions.
“The thing that is most important is that mucin-type glycosylation can regulate various cellular functions [39].”
From Chemical Variability and Biological Potential of Cornu aspersum Mucus as a Source for the Development of New Cosmetic and Pharmaceutical Products (2025) · cites this paper as [39]
The mucin-dominant glycocalyx is believed to act as a barrier against pathogens.
“The mucin-dominant glycocalyx is believed to act as a barrier against pathogens [13,39].”
From Chemical Variability and Biological Potential of Cornu aspersum Mucus as a Source for the Development of New Cosmetic and Pharmaceutical Products (2025) · cites this paper as [39]
Glycoproteins with a mucin domain define an extracellular microenvironment with a high density and molecular weight of their associated glycans (up to 80-90 percent of the total glycoprotein mass), which form the main component of glycocalyx.
“Glycoproteins with a mucin domain define an extracellular microenvironment with a high density and molecular weight of their associated glycans (up to 80–90 percent of the total glycoprotein mass), which form the main component of glycocalyx.”
From Chemical Variability and Biological Potential of Cornu aspersum Mucus as a Source for the Development of New Cosmetic and Pharmaceutical Products (2025) · cites this paper as [39]
The length of the glycosylation domain and the number of repeats are individual for different mucins and determine their chemical and biological properties.
“The length of the glycosylation domain and the number of repeats are individual for different mucins and determine their chemical and biological properties.”
From Chemical Variability and Biological Potential of Cornu aspersum Mucus as a Source for the Development of New Cosmetic and Pharmaceutical Products (2025) · cites this paper as [39]
A mucin molecule consists of a long peptide chain (apomucin) and several hundred oligosaccharide chains attached to it; its central PTS/VNTR domain rich in serine, threonine, and proline serves as an anchor for glycosylation; the mucin adopts an extended bottle brush conformation and cysteine-rich sites form disulfide bonds.
“A mucin molecule consists of a long peptide chain (apomucin) and several hundred oligosaccharide chains attached to it. In the center of the protein backbone, there is a tandem repeat domain rich in serine, threonine, and proline, which is called the PTS (proline, threonine, serine) or VNTR (Variable Number Tandem Repeat) region. This domain serves as an anchor for glycosylation. The PTS domain is”
From Chemical Variability and Biological Potential of Cornu aspersum Mucus as a Source for the Development of New Cosmetic and Pharmaceutical Products (2025) · cites this paper as [39]
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Hudz, N., Turkina, V., Alyokhina, T., Motyka, O., Chemerys, N., Rumynska, T., Lozynskyi, A., Jasicka-Misiak, I., & Kobylinska, L. (2025) · Molecules · doi:10.3390/molecules30214197 · Cited by 4 · see citing works
- Authors
- Ince, D., Lucas, T. M., & Malaker, S. A.
- Affiliations
- Yale University (US)
- Corresponding author
- Malaker, Stacy A.
- Venue
- Current Opinion in Chemical Biology
- Publisher
- Elsevier BV
- Published
- 2022-08
- Volume
- 69
- Pages
- 102174
- ISSN
- 1367-5931 (ISSN-L)
- OpenAlex
- W4283372586
- Cited by
- 51
- References
- 0
- Citations by year
- 2026: 11 · 2025: 14 · 2024: 11 · 2023: 14 · 2022: 1
- FWCI
- 1.05
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Current Opinion in Chemical Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Keywords
- mucin, O-glycosylation, post-translational modification, mucinase, glycoproteomics, synthetic glycopeptides, glycan structure
- MeSH terms
- Glycopeptides, Glycoproteins, Glycosylation, Mucins, Polysaccharides
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