Definition and research guide
This page combines a MeSH definition, publication statistics and selected research abstracts. It is a starting point for reading the literature, not a medical textbook or a systematic evidence review.
Content available: 4 complete abstracts (736 words), 10 references. Full article text is not stored or reproduced here; follow the PMID, DOI or PMC links to read the original sources and their access terms.
Definition
High molecular weight mucoproteins that protect the surface of epithelial cells by providing a barrier to particulate matter and microorganisms. Membrane-anchored mucins may have additional roles concerned with protein interactions at the cell surface.
Definition: NLM Medical Subject Headings (MeSH) scope note (Public domain (U.S. National Library of Medicine); attribution requested). View the MeSH record.
Also known as: Mucin.
Where it fits in the MeSH classification
- Broader topics
- Mucoproteins
- Narrower topics
- CA-125 Antigen; Gastric Mucins; Mucin-1; Mucin-2; Mucin-3; Mucin-4; Mucin-5B; Sialomucins
Related concepts
- Epithelial Cells
Research landscape
PubMed indexes 30,654 records tagged with the MeSH heading “Mucins” (counts retrieved 2026-10-31). 5,006 of them (16.3%) were published from 2020 onward, and the busiest period so far is 2010-2019 with 8,928 records.
Reviews account for 2,674 records (8.7%) and meta-analyses for 128. Randomized controlled trials number 280 (0.9%) as a share of all records on the topic. Randomized trials make up only a small share of this literature, so much of what is known comes from laboratory, observational or descriptive work.
Show the data
| Period | Records |
|---|---|
| through 1999 | 8,864 |
| 2000-2009 | 7,856 |
| 2010-2019 | 8,928 |
| 2020 onward | 5,006 |
Publication-type chart data
| Type | Records | Share |
|---|---|---|
| Reviews | 2,674 | 8.7% |
| Meta-analyses | 128 | 0.4% |
| Randomized controlled trials | 280 | 0.9% |
Method: PubMed query "Mucins"[MeSH Terms] with publication-type and date filters, retrieved 2026-10-31.
Reading the evidence in drugs and chemicals
Studies of a chemical or drug can answer very different questions: what it is and how it behaves in cells and animals, how the body handles it, and whether it changes outcomes in people. Laboratory and animal findings often do not carry over to patients, and observational studies of exposures are confounded by who uses a substance and why. Nothing on this page is a recommendation to use, avoid, start or stop any substance or medicine; talk to a qualified clinician or pharmacist about your own situation. Check the dose, the species, the comparison group and whether a patient-relevant outcome was measured.
Evidence from open-access studies
These open-access studies come from PubMed’s best-match results for this heading (papers whose main topic it is), ranked here by citation count, with one recent addition. Each abstract is reproduced in full under its recorded open licence so that you can read the authors’ own words. They illustrate the literature; they are not a systematic summary of it. Citation counts measure attention, not reliability or clinical benefit.
Carbohydrate-active enzymes from Akkermansia muciniphila break down mucin O-glycans to completion [1]
Abstract reading summary — source excerpts
- Opening excerpt
- Akkermansia muciniphila is a human microbial symbiont residing in the mucosal layer of the large intestine.
- Closing excerpt
- muciniphila.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (165 words)
Akkermansia muciniphila is a human microbial symbiont residing in the mucosal layer of the large intestine. Its main carbon source is the highly heterogeneous mucin glycoprotein, and it uses an array of carbohydrate-active enzymes and sulfatases to access this complex energy source. Here we describe the biochemical characterization of 54 glycoside hydrolases, 11 sulfatases and 1 polysaccharide lyase from A. muciniphila to provide a holistic understanding of their carbohydrate-degrading activities. This was achieved using a variety of liquid chromatography techniques, mass spectrometry, enzyme kinetics and thin-layer chromatography. These results are supported with A. muciniphila growth and whole-cell assays. We find that these enzymes can act synergistically to degrade the O-glycans on the mucin polypeptide to completion, down to the core N-acetylgalactosaime. In addition, these enzymes can break down human breast milk oligosaccharide, ganglioside and globoside glycan structures, showing their capacity to target a variety of host glycans. These data provide a resource to understand the full degradative capability of the gut microbiome member A. muciniphila.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 39891011 · DOI · PMC11790493
Breaking down barriers: is intestinal mucus degradation by Akkermansia muciniphila beneficial or harmful? [2]
Abstract reading summary — source excerpts
- Opening excerpt
- Akkermansia muciniphila is a specialized mucin-degrading bacterium that plays a pivotal role in gut health and disease.
- Closing excerpt
- This review aims to provide a balanced perspective on the implications of gut microbial mucus degradation, highlighting that it can be good, and it can be bad depending on the context.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (230 words)
Akkermansia muciniphila is a specialized mucin-degrading bacterium that plays a pivotal role in gut health and disease. This review examines the dualistic nature of A. muciniphila mucin degradation, exploring its potential benefits and risks. As a mucin specialist, A. muciniphila uses glycosyl hydrolases and mucinases to degrade mucins, producing metabolites like short-chain fatty acids (SCFAs), branched-chain fatty acids (BCFAs), succinate, and other compounds. These metabolites benefit host health and cross-feed other commensal microbes, such as butyrate producers. A. muciniphila levels are inversely correlated with several disease states, such as obesity, diabetes, and inflammatory states, and administration of A. muciniphila has been found by several groups to restore and maintain gut homeostasis. However, under certain conditions, such as low dietary fiber or conditions with an altered gut microbiota, excessive mucin degradation by A. muciniphila can compromise the mucus barrier, increasing susceptibility to inflammation, infection, and pathogenic overgrowth. Elevated A. muciniphila levels have been associated with various diseases and medications, including graft versus host disease (GVHD) and irradiation, and shown to exacerbate infections by enteric pathogens. The context-dependent effects of A. muciniphila and mucin degradation underscore the need for a nuanced understanding of its interactions with the host and microbial community. This review aims to provide a balanced perspective on the implications of gut microbial mucus degradation, highlighting that it can be good, and it can be bad depending on the context.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 40788133 · DOI · PMC12418764
A Bacteroides thetaiotaomicron genetic locus encodes activities consistent with mucin O-glycoprotein processing and N-acetylgalactosamine metabolism [3]
Abstract reading summary — source excerpts
- Opening excerpt
- The gut microbiota is a key modulator of human health and the status of major diseases including cancer, diabetes and inflammatory bowel disease.
- Closing excerpt
- These data advance our understanding of glycoprotein metabolism at mucosal surfaces, highlighting GalNAc as a key metabolite for competitive microbial survival in the human gut.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (189 words)
The gut microbiota is a key modulator of human health and the status of major diseases including cancer, diabetes and inflammatory bowel disease. Central to microbiota survival is the ability to metabolise complex dietary and host-derived glycans, including intestinal mucins. The prominent human gut microbe Bacteroides thetaiotaomicron (B. theta) is a versatile and highly efficient complex glycan degrader thanks to the expansion of gene clusters termed polysaccharide utilisation loci (PULs). While the mechanism of action for several singular dietary glycan-induced PULs have been elucidated, studies on the unusually high number of mucin-inducible PULs in B. theta significantly lag behind. Here we show that a mucin inducible PUL BT4240-50 encodes activities consistent with the processing and metabolism of mucin O-glycoproteins and their core sugar N-acetylgalactosamine (GalNAc). PUL BT4240-50 was also shown to be important for competitive growth on mucins in vitro, encoding a kinase (BT4240) critical for GalNAc metabolism. Additionally, BT4240-kinase was shown to be essential for glycosaminoglycan metabolism, extending the PULs function beyond mucins. These data advance our understanding of glycoprotein metabolism at mucosal surfaces, highlighting GalNAc as a key metabolite for competitive microbial survival in the human gut.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 40216766 · DOI · PMC11992087
The receptor binding properties of H5Ny influenza A viruses have evolved to bind to avian-type mucin-like O-glycans [4]
Abstract reading summary — source excerpts
- Opening excerpt
- Highly pathogenic H5Ny influenza A viruses are causing unprecedented, season-independent outbreaks across avian and mammalian species, including dairy cattle, a novel reservoir.
- Closing excerpt
- While these viruses do not bind human-type receptors, their broad receptor specificity enhances binding to human tracheal tissues, suggesting that O-glycan recognition could contribute to the continues spillover of this clade.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (152 words)
Highly pathogenic H5Ny influenza A viruses are causing unprecedented, season-independent outbreaks across avian and mammalian species, including dairy cattle, a novel reservoir. The sialoside-binding properties of influenza A hemagglutinin (HA) are strongly related to its ability to infect and transmit between hosts. Mucin-like O-glycans, omnipresent in respiratory tracts, have been understudied as viral receptors due to their complexity. To address this, we synthesized 25 O-linked glycans with diverse sialosides, including modifications by fucosides and sulfates. Our findings reveal that H5Ny 2.3.4.4b viruses bind core 3 sialyl-Lewisx and Sia-Gal-β3GalNAc, O-linked glycans not recognized by classical H5 or other avian viruses. By determining crystal structures, we resolved the structural features of four glycans in an H5 hemagglutinin (HA) from a 2016 2.3.4.4b virus. While these viruses do not bind human-type receptors, their broad receptor specificity enhances binding to human tracheal tissues, suggesting that O-glycan recognition could contribute to the continues spillover of this clade.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 41557749 · DOI · PMC12904578
Key reviews and meta-analyses
The most cited review-type papers among PubMed’s best-match results for this heading, listed with bibliographic details only. Follow the links for the full text and access terms.
- Research article Mucus barrier, mucins and gut microbiota: the expected slimy partners? [5]
- Research article The mucus and mucins of the goblet cells and enterocytes provide the first defense line of the gastrointestinal tract and interact with the immune system [6]
- Research article Immunological aspects of intestinal mucus and mucins [7]
- Research article MUC1: a multifaceted oncoprotein with a key role in cancer progression [8]
- Research article Definitions for response and progression in ovarian cancer clinical trials incorporating RECIST 1.1 and CA 125 agreed by the Gynecological Cancer Intergroup (GCIG) [9]
- Research article Biomarkers and algorithms for diagnosis of ovarian cancer: CA125, HE4, RMI and ROMA, a review [10]
References
- Bakshani CR, Ojuri TO, Pilgaard B, Holck J, McInnes R, Kozak RP, et al.. Carbohydrate-active enzymes from Akkermansia muciniphila break down mucin O-glycans to completion. . 2025. PMID 39891011 · DOI · PMC11790493
- Tingler AM, Engevik MA. Breaking down barriers: is intestinal mucus degradation by Akkermansia muciniphila beneficial or harmful?. . 2025. PMID 40788133 · DOI · PMC12418764
- Ndeh DA, Nakjang S, Kwiatkowski KJ, Sawyers C, Koropatkin NM, Hirt RP, et al.. A Bacteroides thetaiotaomicron genetic locus encodes activities consistent with mucin O-glycoprotein processing and N-acetylgalactosamine metabolism. . 2025. PMID 40216766 · DOI · PMC11992087
- Weber J, Ponse NLD, Zhu X, Ríos Carrasco M, Han AX, Funk M, et al.. The receptor binding properties of H5Ny influenza A viruses have evolved to bind to avian-type mucin-like O-glycans. . 2026. PMID 41557749 · DOI · PMC12904578
- Paone P, Cani PD. Mucus barrier, mucins and gut microbiota: the expected slimy partners?. Gut. 2020. PMID 32917747 · DOI · PMC7677487
- Pelaseyed T, Bergström JH, Gustafsson JK, Ermund A, Birchenough GM, Schütte A, et al.. The mucus and mucins of the goblet cells and enterocytes provide the first defense line of the gastrointestinal tract and interact with the immune system. Immunol Rev. 2014. PMID 24942678 · DOI · PMC4281373
- Johansson ME, Hansson GC. Immunological aspects of intestinal mucus and mucins. Nat Rev Immunol. 2016. PMID 27498766 · DOI · PMC6435297
- Nath S, Mukherjee P. MUC1: a multifaceted oncoprotein with a key role in cancer progression. Trends Mol Med. 2014. PMID 24667139 · DOI · PMC5500204
- Rustin GJ, Vergote I, Eisenhauer E, Pujade-Lauraine E, Quinn M, Thigpen T, et al.. Definitions for response and progression in ovarian cancer clinical trials incorporating RECIST 1.1 and CA 125 agreed by the Gynecological Cancer Intergroup (GCIG). Int J Gynecol Cancer. 2011. PMID 21270624 · DOI
- Dochez V, Caillon H, Vaucel E, Dimet J, Winer N, Ducarme G. Biomarkers and algorithms for diagnosis of ovarian cancer: CA125, HE4, RMI and ROMA, a review. J Ovarian Res. 2019. PMID 30917847 · DOI · PMC6436208
About this article
- Sources
- NLM Medical Subject Headings (definition, synonyms); NCBI PubMed (counts, identifiers); Europe PMC (open-access abstracts and citation counts).
- Verification
- Every reference was resolved against PubMed on 2026-10-31; title, year and DOI matched.
- Review state
- automated source verified; no human expert review has been recorded yet.
- Version
- 1, last updated 2026-10-31.
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Evidence strength
EvidenceHelix's computed view of the study designs behind this topic: how common meta-analyses, randomized trials and reviews are, how recent the literature is, and a plain-language reading. It describes the design mix of the literature. It is not a quality appraisal of any study, and it is not medical advice.