ArticleInfection and immunity2016
The Cryptosporidium parvum C-Type Lectin CpClec Mediates Infection of Intestinal Epithelial Cells via Interactions with Sulfated Proteoglycans.
Article in Infection and immunity, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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Who cites it
23 citing papers in PubMed, 33 citations in OpenAlex.
- Pathogenicity and virulence ofVirulence · 2025Review
- Deciphering Host-Pathogen Interactions: Role ofPathogens (Basel, Switzerland) · 2025Review
- Vaccination of mice with Trichinella spiralis C-type lectin elicited the protective immunity and enhanced gut epithelial barrier function.PLoS neglected tropical diseases · 2025Article
- Multicopy subtelomeric genes underlie animal infectivity of divergent Cryptosporidium hominis subtypes.Nature communications · 2024Article
- Pathogen-binding nanoparticles to inhibit host cell infection by heparan sulfate and sialic acid dependent viruses and protozoan parasites.Smart medicine · 2024Review
- Sequence introgression from exogenous lineages underlies genomic and biological differences among Cryptosporidium parvum IOWA lines.Water research · 2024Article
- A single-pass type I membrane protein, mannose-specific L-type lectin, potentially involved in the adhesion and invasion of Cryptosporidium parvum.Parasite (Paris, France) · 2024Article
- Binding of Trichinella spiralis C-type lectin with syndecan-1 on intestinal epithelial cells mediates larval invasion of intestinal epithelium.Veterinary research · 2023Article
- Effect of Glycosaminoglycans onApplied and environmental microbiology · 2023Article
- Multiple introductions and recombination events underlie the emergence of a hyper-transmissible Cryptosporidium hominis subtype in the USA.Cell host & microbe · 2023Article
- A novel C-type lectin from Trichinella spiralis mediates larval invasion of host intestinal epithelial cells.Veterinary research · 2022Article
- A genetic screen identifies a protective type III interferon response to Cryptosporidium that requires TLR3 dependent recognition.PLoS pathogens · 2022Article
- The Oesophageal Squamous Cell Carcinoma Cell Line COLO-680N Fails to Support SustainedPathogens (Basel, Switzerland) · 2021Article
- Implications of Glycosaminoglycans on Viral Zoonotic Diseases.Diseases (Basel, Switzerland) · 2021Review
- Establishment of a Newborn Lamb Gut-Loop Model to Evaluate New Methods of Enteric Disease Control and Reduce Experimental Animal Use.Veterinary sciences · 2021Article
- A Single-Pass Type I Membrane Protein from the Apicomplexan ParasiteMicroorganisms · 2021Article
- Interaction between human mucins and parasite glycoproteins: the role of lectins and glycosidases in colonization by intestinal protozoa.Revista do Instituto de Medicina Tropical de Sao Paulo · 2020Article
- Identification and preliminary characterization of Hc-clec-160, a novel C-type lectin domain-containing gene of the strongylid nematode Haemonchus contortus.Parasites & vectors · 2018Article
- Fluorescent Tracking of Yeast Division Clarifies the Essential Role of Spleen Tyrosine Kinase in the Intracellular Control ofFrontiers in immunology · 2018Article
- Complete cryspovirus genome sequences from Cryptosporidium parvum isolate Iowa.Archives of virology · 2017Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The apicomplexan parasite Cryptosporidium causes significant diarrheal disease worldwide. Effective anticryptosporidial agents are lacking, in part because the molecular mechanisms underlying Cryptosporidium-host cell interactions are poorly understood. Previously, we identified and characterized a novel Cryptosporidium parvum C-type lectin domain-containing mucin-like glycoprotein, CpClec. In this study, we evaluated the mechanisms underlying interactions of CpClec with intestinal epithelial cells by using an Fc-tagged recombinant protein. CpClec-Fc displayed Ca(2+)-dependent, saturable binding to HCT-8 and Caco-2 cells and competitively inhibited C. parvum attachment to and infection of HCT-8 cells. Binding of CpClec-Fc was specifically inhibited by sulfated glycosaminoglycans, particularly heparin and heparan sulfate. Binding was reduced after the removal of heparan sulfate and following the inhibition of glycosaminoglycan synthesis or sulfation in HCT-8 cells. Like CpClec-Fc binding, C. parvum attachment to and infection of HCT-8 cells were inhibited by glycosaminoglycans and were reduced after heparan sulfate removal or inhibition of glycosaminoglycan synthesis or sulfation. Lastly, CpClec-Fc binding and C. parvum sporozoite attachment were significantly decreased in CHO cell mutants defective in glycosaminoglycan synthesis. Together, these results indicate that CpClec is a novel C-type lectin that mediates C. parvum attachment and infection via Ca(2+)-dependent binding to sulfated proteoglycans on intestinal epithelial cells.
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Registered trials
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