ArticlePloS one2012
A novel PAN/apple domain-containing protein from Toxoplasma gondii: characterization and receptor identification.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 34 citations in OpenAlex.
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- How does Toxoplama gondii invade host cells?The Journal of veterinary medical science · 2018Review
- Characterization of a Toxoplasma gondii calcium calmodulin-dependent protein kinase homolog.Parasites & vectors · 2016Article
- The Cryptosporidium parvum C-Type Lectin CpClec Mediates Infection of Intestinal Epithelial Cells via Interactions with Sulfated Proteoglycans.Infection and immunity · 2016Article
- Dextran sulfate inhibits acute Toxoplama gondii infection in pigs.Parasites & vectors · 2016Article
- The role of carbohydrates in infection strategies of enteric pathogens.Tropical medicine and health · 2015Review
- Effects of dextran sulfates on the acute infection and growth stages of Toxoplasma gondii.Parasitology research · 2013Article
- Development of 116 kDa Fraction for Detecting Experimental Toxoplasma gondii Infections in Mice.Iranian journal of parasitology · 2013Article
- SAG2A protein from Toxoplasma gondii interacts with both innate and adaptive immune compartments of infected hosts.Parasites & vectors · 2013Article
- Global proteomic analysis of the oocyst/sporozoite of Toxoplasma gondii reveals commitment to a host-independent lifestyle.BMC genomics · 2013Article
- The unique architecture and function of cellulose-interacting proteins in oomycetes revealed by genomic and structural analyses.BMC genomics · 2012Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Toxoplasma gondii is an intracellular parasite that invades nucleated cells, causing toxoplasmosis in humans and animals worldwide. The extremely wide range of hosts susceptible to T. gondii is thought to be the result of interactions between T. gondii ligands and receptors on its target cells. In this study, a host cell-binding protein from T. gondii was characterized, and one of its receptors was identified. P104 (GenBank Access. No. CAJ20677) is 991 amino acids in length, containing a putative 26 amino acid signal peptide and 10 PAN/apple domains, and shows low homology to other identified PAN/apple domain-containing molecules. A 104-kDa host cell-binding protein was detected in the T. gondii lysate. Immunofluorescence assays detected P104 at the apical end of extracellular T. gondii. An Fc-fusion protein of the P104 N-terminus, which contains two PAN/apple domains, showed strong affinity for the mammalian and insect cells evaluated. This binding was not related to protein-protein or protein-lipid interactions, but to a protein-glycosaminoglycan (GAG) interaction. Chondroitin sulfate (CS), a kind of GAG, was shown to be involved in adhesion of the Fc-P104 N-terminus fusion protein to host cells. These results suggest that P104, expressed at the apical end of the extracellular parasite, may function as a ligand in the attachment of T. gondii to CS or other receptors on the host cell, facilitating invasion by the parasite.
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