ArticlePloS one2017
Cryptosporidium parvum vaccine candidates are incompletely modified with O-linked-N-acetylgalactosamine or contain N-terminal N-myristate and S-palmitate.
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 25 citations in OpenAlex.
- A comprehensive proteome and the first phosphoproteome reveal extensive phosphorylation of carbohydrate metabolism in Cryptosporidium parvum sporozoites.Parasites & vectors · 2026Article
- Mouse Models for Use in Cryptosporidium Infection Studies, Quantification of Parasite Burden Using Flow Cytometry, qPCR and Histopathology, and Confocal Imaging of Oocysts.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Pathogenicity and virulence ofVirulence · 2025Review
- Targeted CRISPR screens reveal genes essential for Cryptosporidium survival in the host intestine.Nature communications · 2025Article
- Cellulose binding and the timing of expression influence protein targeting to the double-layered cyst wall ofmSphere · 2024Article
- Identification of the glycopeptide epitope recognized by a protectiveInfection and immunity · 2023Article
- Specific Cryptosporidium antigens associate with reinfection immunity and protection from cryptosporidiosis.The Journal of clinical investigation · 2023Article
- Association between socioeconomic deprivation and incidence of infectious intestinal disease by pathogen and linked transmission route: An ecological analysis in the UK.Epidemiology and infection · 2023Article
- Conservation, abundance, glycosylation profile, and localization of the TSP protein family in Cryptosporidium parvum.The Journal of biological chemistry · 2023Article
- The mucin-like, secretory type-I transmembrane glycoprotein GP900 in the apicomplexan Cryptosporidium parvum is cleaved in the secretory pathway and likely plays a lubrication role.Parasites & vectors · 2022Article
- Genomic reconstruction and features of glycosylation pathways in the apicomplexanFrontiers in molecular biosciences · 2022Review
- Identification and characterization of a new 34 kDa MORN motif-containing sporozoite surface-exposed protein, Cp-P34, unique to Cryptosporidium.International journal for parasitology · 2021Article
- Glycopeptidomics Analysis of a Cell Line Model Revealing Pathogenesis and Potential Marker Molecules for the Early Diagnosis of Gastric MALT Lymphoma.Frontiers in cellular and infection microbiology · 2021Article
- ProteinParasitology · 2019Review
- Comparative Pathobiology of the Intestinal Protozoan ParasitesPathogens (Basel, Switzerland) · 2019Review
- Opportunistic parasitic infections in patients with human immunodeficiency virus/acquired immunodeficiency syndrome: A review.Veterinary world · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Cryptosporidium parvum (studied here) and Cryptosporidium hominis are important causes of diarrhea in infants and immunosuppressed persons. C. parvum vaccine candidates, which are on the surface of sporozoites, include glycoproteins with Ser- and Thr-rich domains (Gp15, Gp40, and Gp900) and a low complexity, acidic protein (Cp23). Here we used mass spectrometry to determine that O-linked GalNAc is present in dense arrays on a glycopeptide with consecutive Ser derived from Gp40 and on glycopeptides with consecutive Thr derived from Gp20, a novel C. parvum glycoprotein with a formula weight of ~20 kDa. In contrast, the occupied Ser or Thr residues in glycopeptides from Gp15 and Gp900 are isolated from one another. Gly at the N-terminus of Cp23 is N-myristoylated, while Cys, the second amino acid, is S-palmitoylated. In summary, C. parvum O-GalNAc transferases, which are homologs of host enzymes, densely modify arrays of Ser or Thr, as well as isolated Ser and Thr residues on C. parvum vaccine candidates. The N-terminus of an immunodominant antigen has lipid modifications similar to those of host cells and other apicomplexan parasites. Mass spectrometric demonstration here of glycopeptides with O-glycans complements previous identification C. parvum O-GalNAc transferases, lectin binding to vaccine candidates, and human and mouse antibodies binding to glycopeptides. The significance of these post-translational modifications is discussed with regards to the function of these proteins and the design of serological tests and vaccines.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.