ArticleInfection and immunity2013
Identification and characterization of Cryptosporidium parvum Clec, a novel C-type lectin domain-containing mucin-like glycoprotein.
Article in Infection and immunity, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 30 citations in OpenAlex.
- Pathogenicity and virulence ofVirulence · 2025Review
- Descriptive analysis of protein expression variations during pupal development ofForensic sciences research · 2025Article
- Cryptosporidiosis: A global threat to human and animal health.Open veterinary journal · 2025Review
- Influence of pH, ion composition and carbohydrate recognition on the attachment ofCurrent research in parasitology & vector-borne diseases · 2025Article
- Article
- Identification of the glycopeptide epitope recognized by a protectiveInfection and immunity · 2023Article
- Discovery of New Microneme Proteins inFrontiers in veterinary science · 2021Article
- Review
- 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
- Mucins and Pathogenic Mucin-Like Molecules Are Immunomodulators During Infection and Targets for Diagnostics and Vaccines.Frontiers in chemistry · 2019Review
- Characterization of a Species-Specific Insulinase-Like Protease inFrontiers in microbiology · 2019Article
- Diverse single-amino-acid repeat profiles in the genus Cryptosporidium.Parasitology · 2018Article
- 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
- A cell culture platform for Cryptosporidium that enables long-term cultivation and new tools for the systematic investigation of its biology.International journal for parasitology · 2018Article
- Immunolocation and enzyme activity analysis of Cryptosporidium parvum enolase.Parasites & vectors · 2017Article
- A multigene family encoding surface glycoproteins inMicrobial cell (Graz, Austria) · 2017Article
- The Cryptosporidium parvum C-Type Lectin CpClec Mediates Infection of Intestinal Epithelial Cells via Interactions with Sulfated Proteoglycans.Infection and immunity · 2016Article
- Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Cryptosporidium species are waterborne apicomplexan parasites that cause diarrheal disease worldwide. Although the mechanisms underlying Cryptosporidium-host cell interactions are not well understood, mucin-like glycoproteins of the parasite are known to mediate attachment and invasion in vitro. We identified C. parvum Clec (CpClec), a novel mucin-like glycoprotein that contains a C-type lectin domain (CTLD) and has orthologs in C. hominis and C. muris. CTLD-containing proteins are ligand-binding proteins that function in adhesion and signaling and are present in a wide range of organisms, from humans to viruses. However, this is the first report of a CTLD-containing protein in protozoa and in Apicomplexa. CpClec is predicted to be a type 1 membrane protein, with a CTLD, an O-glycosylated mucin-like domain, a transmembrane domain, and a cytoplasmic tail containing a YXX sorting motif. The predicted structure of CpClec displays several characteristics of canonical CTLD-containing proteins, including a long loop region hydrophobic core associated with calcium-dependent glycan binding as well as predicted calcium- and glycan-binding sites. CpClec expression during C. parvum infection in vitro is maximal at 48 h postinfection, suggesting that it is developmentally regulated. The 120-kDa mass of native CpClec is greater than predicted, most likely due to O-glycosylation. CpClec is localized to the surface of the apical region and to dense granules of sporozoites and merozoites. Taken together, these findings, along with the known functions of C. parvum mucin-like glycoproteins and of CTLD-containing proteins, strongly implicate a significant role for CpClec in Cryptosporidium-host cell interactions.
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