ArticleThe Journal of biological chemistry2013
Elongation factor-1α is a novel protein associated with host cell invasion and a potential protective antigen of Cryptosporidium parvum.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 48 citations in OpenAlex.
- Evaluation of Immunoprotective Effects of DNA Vaccine Based onAnimals : an open access journal from MDPI · 2026Article
- Comparative Analysis of the EF-1α Intergenic Region inInternational journal of molecular sciences · 2026Article
- Characterization of antigenic proteins of the Taenia solium postoncospheral form.Molecular and biochemical parasitology · 2024Article
- RNA-Seq of Phenotypically DistinctPathogens (Basel, Switzerland) · 2023Article
- Protective efficacy of multiepitope vaccines constructed from common antigens of Eimeria species in chickens.Veterinary research · 2023Article
- Protection againstInfection and immunity · 2023Article
- Specific Cryptosporidium antigens associate with reinfection immunity and protection from cryptosporidiosis.The Journal of clinical investigation · 2023Article
- Eimeria falciformis secretes extracellular vesicles to modulate proinflammatory response during interaction with mouse intestinal epithelial cells.Parasites & vectors · 2022Article
- Proteomic Analysis ofPathogens (Basel, Switzerland) · 2022Article
- An Ebola,Computational and structural biotechnology journal · 2021Article
- Evaluation on Elongation Factor 1 Alpha ofPathogens (Basel, Switzerland) · 2020Article
- Recombinant elongation factor 1 alpha of Haemonchus contortus affects the functions of goat PBMCs.Parasite immunology · 2020Article
- A review of Eimeria antigen identification for the development of novel anticoccidial vaccines.Parasitology research · 2019Review
- Differential Expression of ThreeFrontiers in microbiology · 2019Article
- Characterization of a Species-Specific Insulinase-Like Protease inFrontiers in microbiology · 2019Article
- Monoclonal Antibody Preparation and Epitope Identification forFrontiers in microbiology · 2019Article
- Proteomic analysis of protein interactions between Eimeria maxima sporozoites and chicken jejunal epithelial cells by shotgun LC-MS/MS.Parasites & vectors · 2018Article
- Elongation factor Tu is a multifunctional and processed moonlighting protein.Scientific reports · 2017Article
- Characterization of the Activities of Dinuclear Thiolato-Bridged Arene Ruthenium Complexes against Toxoplasma gondii.Antimicrobial agents and chemotherapy · 2017Article
- Immunolocation and enzyme activity analysis of Cryptosporidium parvum enolase.Parasites & vectors · 2017Article
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Authors and funding
8 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The phylum Apicomplexa comprises obligate intracellular parasites that infect vertebrates. All invasive forms of Apicomplexa possess an apical complex, a unique assembly of organelles localized to the anterior end of the cell and involved in host cell invasion. Previously, we generated a chicken monoclonal antibody (mAb), 6D-12-G10, with specificity for an antigen located in the apical cytoskeleton of Eimeria acervulina sporozoites. This antigen was highly conserved among Apicomplexan parasites, including other Eimeria spp., Toxoplasma, Neospora, and Cryptosporidium. In the present study, we identified the apical cytoskeletal antigen of Cryptosporidium parvum (C. parvum) and further characterized this antigen in C. parvum to assess its potential as a target molecule against cryptosporidiosis. Indirect immunofluorescence demonstrated that the reactivity of 6D-12-G10 with C. parvum sporozoites was similar to those of anti-β- and anti-γ-tubulins antibodies. Immunoelectron microscopy with the 6D-12-G10 mAb detected the antigen both on the sporozoite surface and underneath the inner membrane at the apical region of zoites. The 6D-12-G10 mAb significantly inhibited in vitro host cell invasion by C. parvum. MALDI-TOF/MS and LC-MS/MS analysis of tryptic peptides revealed that the mAb 6D-12-G10 target antigen was elongation factor-1α (EF-1α). These results indicate that C. parvum EF-1α plays an essential role in mediating host cell entry by the parasite and, as such, could be a candidate vaccine antigen against cryptosporidiosis.
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