ArticleProceedings of the National Academy of Sciences of the United States of America2006
Entamoeba histolytica cysteine proteases cleave the MUC2 mucin in its C-terminal domain and dissolve the protective colonic mucus gel.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 130 papers.
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130 citing papers in PubMed, 256 citations in OpenAlex.
- A multifaceted model of Entamoeba histolytica KERP2 regulating gene expression and host cell responses.Nature communications · 2026Article
- Structural basis for carbohydrate recognition by the Gal/GalNAc lectin of Entamoeba histolytica involved in host cell adhesion.PLoS pathogens · 2026Article
- Roles of Glycoconjugates and Mucinases from Carcinogenic Liver Fluke, Opisthorchis viverrini, in Host: Parasite Interactions.Advances in experimental medicine and biology · 2026Review
- EatA mediated degradation of intestinal mucus is species-specific and driven by MUC2 structural features.Nature communications · 2025Article
- Pathogenicity and virulence ofVirulence · 2025Review
- Cross-species protection suggestsInfection and immunity · 2025Article
- Human Mucin-2-Producing Colonic Goblet-Like Cells Secrete the Chemokine CXCL8 by Activating Multiple Proinflammatory Pathways in Response to Entamoeba histolytica.The American journal of pathology · 2025Article
- Mucins and Their Roles in Asthma.Immunological reviews · 2025Review
- Cultivating complexity: Advancements in establishing in vitro models for the mucus-adhering gut microbiota.Microbial biotechnology · 2024Review
- Oral infectivity through carnivorism in murine model ofFrontiers in cellular and infection microbiology · 2024Article
- Pathogenicity and virulence ofVirulence · 2023Review
- Article
- Molecular characterisation of Entamoeba histolytica UDP-glucose 4-epimerase, an enzyme able to provide building blocks for cyst wall formation.PLoS neglected tropical diseases · 2023Article
- Diversity and Plasticity of Virulent Characteristics ofTropical medicine and infectious disease · 2023Review
- Intestinal mucus components and secretion mechanisms: what we do and do not know.Experimental & molecular medicine · 2023Review
- Variations in active proteases ofJournal of parasitic diseases : official organ of the Indian Society for Parasitology · 2022Article
- Mucus interaction to improve gastrointestinal retention and pharmacokinetics of orally administered nano-drug delivery systems.Journal of nanobiotechnology · 2022Review
- Defining the early stages of intestinal colonisation by whipworms.Nature communications · 2022Article
- Gasdermins in Innate Host Defense AgainstFrontiers in immunology · 2022Review
- Mucus and Mucins: The Underappreciated Host Defence System.Frontiers in cellular and infection microbiology · 2022Review
70 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In order for the protozoan parasite Entamoeba histolytica (E.h.) to cause invasive intestinal and extraintestinal infection, which leads to significant morbidity and mortality, it must disrupt the protective mucus layer by a previously unknown mechanism. We hypothesized that cysteine proteases secreted from the amoeba disrupt the mucin polymeric network, thereby overcoming the protective mucus barrier. The MUC2 mucin is the major structural component of the colonic mucus gel. Heavily O-glycosylated and protease-resistant mucin domains characterize gel-forming mucins. Their N- and C-terminal cysteine-rich domains are involved in mucin polymerization, and these domains are likely to be targeted by proteases because they are less glycosylated, thereby exposing their peptide chains. By treating recombinant cysteine-rich domains of MUC2 with proteases from E.h. trophozoites, we showed that the C-terminal domain was specifically targeted at two sites by cysteine proteases, whereas the N-terminal domain was resistant to proteolysis. The major cleavage site is predicted to depolymerize the MUC2 polymers, thereby disrupting the protective mucus gel. The ability of the cysteine proteases to dissolve mucus gels was confirmed by treating mucins from a MUC2-producing cell line with amoeba proteases. These findings suggest a major role for E.h. cysteine proteases in overcoming the protective mucus barrier in the pathogenesis of invasive amoebiasis. In this report, we identify a specific cleavage mechanism used by an enteric pathogen to disrupt the polymeric nature of the mucin gel.
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