ArticlemBio2023
Apical Secretory Glycoprotein Complex Contributes to Cell Attachment and Entry by Cryptosporidium parvum.
Article in mBio, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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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.
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Who cites it
13 citing papers in PubMed, 16 citations in OpenAlex.
- Insights into the lifecycle of Cryptosporidium and compounds targeting developmental stages.Current opinion in microbiology · 2026Review
- Protective Immunity Induced by DNA Vaccines Encoding TgGRA47 and TgGRA72 AgainstTransboundary and emerging diseases · 2026Article
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- Pathogenicity and virulence ofVirulence · 2025Review
- Article
- Secretome and Transcriptome Analyses Reveal New Potential Virulence Factors duringJournal of proteome research · 2025Article
- Independent evolution of holocentric chromosomes in an early branching apicomplexan parasite.bioRxiv : the preprint server for biology · 2025Article
- Cryptosporidium parvum multidrug resistance protein confers resistance to toxic gut microbial metabolite.Cell host & microbe · 2025Article
- Targeted CRISPR screens reveal genes essential for Cryptosporidium survival in the host intestine.Nature communications · 2025Article
- SKSR1 identified as key virulence factor in Cryptosporidium by genetic crossing.Nature communications · 2025Article
- Article
- Mendelian segregation and high recombination rates facilitate genetic analyses in Cryptosporidium parvum.PLoS genetics · 2024Article
- Mendelian segregation and high recombination rates facilitate genetic analyses inbioRxiv : the preprint server for biology · 2024Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Cryptosporidium parvum is an enteric pathogen that invades epithelial cells in the intestine, where it resides at the apical surface in a unique epicellular location. Compared with those of related apicomplexan parasites, the processes of host cell attachment and invasion by C. parvum are poorly understood. The streamlined C. parvum genome contains numerous mucin-like glycoproteins, several of which have previously been shown to mediate cell attachment, although the majority are unstudied. Here, we identified the antigens recognized by monoclonal antibody (MAb) 1A5, which stains the apical end of sporozoites and mature merozoites. Immunoprecipitation with MAb 1A5 followed by mass spectrometry identified a heterodimer comprised of paralogous proteins which are related to additional orthologs in the genome of C. parvum and related species. Paralogous glycoproteins recognized by MAb 1A5 heterodimerize as a complex displayed on the parasite surface, and they also interact with lectins that suggest that they contain mucin-like, O-linked oligosaccharides. Although the gene encoding one of the paralogs was readily disrupted by CRISPR/Cas9 gene editing, its partner, which contains a mucin-like domain related to GP900, was refractory to deletion. Combined with the ability of MAb 1A5 to partially neutralize host cell attachment by sporozoites, these findings define a new family of secretory glycoproteins that participate in cell invasion by
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