ArticleInfection and immunity2000
Mediation of Cryptosporidium parvum infection in vitro by mucin-like glycoproteins defined by a neutralizing monoclonal antibody.
Article in Infection and immunity, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 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
59 citing papers in PubMed.
- Two- and Three-Dimensional Human Intestinal Tissue Models for Cryptosporidium Infection.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Article
- Cryptosporidiosis: A global threat to human and animal health.Open veterinary journal · 2025Review
- Variant surface protein GP60 contributes to host infectivity of Cryptosporidium parvum.Communications biology · 2024Article
- A single-pass type I membrane protein, mannose-specific L-type lectin, potentially involved in the adhesion and invasion of Cryptosporidium parvum.Parasite (Paris, France) · 2024Article
- Functional characterization of CpADF, an actin depolymerizing factor protein in Cryptosporidium parvum.Parasitology research · 2023Article
- 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
- Article
- Article
- Differential Response to the Course of Cryptosporidium parvum Infection and Its Impact on Epithelial Integrity in Differentiated versus Undifferentiated Human Intestinal Enteroids.Infection and immunity · 2022Article
- Global Population Genomics of Two Subspecies of Cryptosporidium hominis during 500 Years of Evolution.Molecular biology and evolution · 2022Article
- A Single-Pass Type I Membrane Protein from the Apicomplexan ParasiteMicroorganisms · 2021Article
- Comparative Study of Two Insulinlike Proteases inMicroorganisms · 2021Article
- Article
- Calcium-Mediated Biophysical Binding of Cryptosporidium parvum Oocysts to Surfaces Is Sensitive to Oocyst Age.Applied and environmental microbiology · 2019Article
- A Stem-Cell-Derived Platform Enables Complete Cryptosporidium Development In Vitro and Genetic Tractability.Cell host & microbe · 2019Article
- Diverse single-amino-acid repeat profiles in the genus Cryptosporidium.Parasitology · 2018Article
- Monoclonal Antibodies to Intracellular Stages of Cryptosporidium parvum Define Life Cycle ProgressionmSphere · 2018Article
- The Apicomplexa-specific glucosamine-6-phosphate N-acetyltransferase gene family encodes a key enzyme for glycoconjugate synthesis with potential as therapeutic target.Scientific reports · 2018Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
The protozoan parasite Cryptosporidium parvum is a significant cause of diarrheal disease worldwide. Attachment to and invasion of host intestinal epithelial cells by C. parvum sporozoites are crucial steps in the pathogenesis of cryptosporidiosis. The molecular basis of these initial interactions is unknown. In order to identify putative C. parvum adhesion- and invasion-specific proteins, we raised monoclonal antibodies (MAbs) to sporozoites and evaluated them for inhibition of attachment and invasion in vitro. Using this approach, we identified two glycoproteins recognized by 4E9, a MAb which neutralized C. parvum infection and inhibited sporozoite attachment to intestinal epithelial cells in vitro. 4E9 recognized a 40-kDa glycoprotein named gp40 and a second, >220-kDa protein which was identified as GP900, a previously described mucin-like glycoprotein. Glycoproteins recognized by 4E9 are localized to the surface and apical region of invasive stages and are shed in trails from the parasite during gliding motility. The epitope recognized by 4E9 contains alpha-N-acetylgalactosamine residues, which are present in a mucin-type O-glycosidic linkage. Lectins specific for these glycans bind to the surface and apical region of sporozoites and block attachment to host cells. The surface and apical localization of these glycoproteins and the neutralizing effect of the MAb and alpha-N-acetylgalactosamine-specific lectins strongly implicate these proteins and their glycotopes as playing a role in C. parvum-host cell interactions.
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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.