ArticleEukaryotic cell2012
The Giardia median body protein is a ventral disc protein that is critical for maintaining a domed disc conformation during attachment.
Article in Eukaryotic cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed.
- Article
- A novel mechanism of microbial attachment: The flagellar pump ofPNAS nexus · 2024Article
- The retromer and retriever systems are conserved and differentially expanded in parabasalids.Journal of cell science · 2024Article
- Characterization of a unique attachment organelle: Single-cell force spectroscopy ofNanoscale · 2024Article
- Ultrastructural Alterations of the Human PathogenPathogens (Basel, Switzerland) · 2023Review
- The Giardia ventrolateral flange is a lamellar membrane protrusion that supports attachment.PLoS pathogens · 2022Article
- Disc and Actin Associated Protein 1 influences attachment in the intestinal parasite Giardia lamblia.PLoS pathogens · 2022Article
- Proteomic Analysis of Trichomonas vaginalis Phagolysosome, Lysosomal Targeting, and Unconventional Secretion of Cysteine Peptidases.Molecular & cellular proteomics : MCP · 2022Article
- Disc-associated proteins mediate the unusual hyperstability of the ventral disc inJournal of cell science · 2020Article
- Recent advances in functional research in Giardia intestinalis.Advances in parasitology · 2020Review
- Microtubule organelles in Giardia.Advances in parasitology · 2020Review
- Article
- Role of gamma-giardin in ventral disc formation of Giardia lamblia.Parasites & vectors · 2019Article
- Robust and stable transcriptional repression in Giardia using CRISPRi.Molecular biology of the cell · 2019Article
- 'Disc-o-Fever': Getting Down with Giardia's Groovy Microtubule Organelle.Trends in cell biology · 2018Review
- Interactions of Giardia sp. with the intestinal barrier: Epithelium, mucus, and microbiota.Tissue barriers · 2017Review
- Identification and Validation of Small-Gatekeeper Kinases as Drug Targets in Giardia lamblia.PLoS neglected tropical diseases · 2016Article
- Identification of a Novel Microtubule-Binding Protein in Giardia lamblia.The Korean journal of parasitology · 2016Article
- A detailed look at the cytoskeletal architecture of the Giardia lamblia ventral disc.Journal of structural biology · 2016Article
- The Critical Role of the Cytoskeleton in the Pathogenesis ofCurrent clinical microbiology reports · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Giardia has unique microtubule structures, including the ventral disc, the primary organelle of attachment to the host, and the median body, a structure of undefined function. During attachment, the ventral disc has a domed conformation and enables Giardia to attach to the host intestinal epithelia within seconds. The mechanism of attachment via the ventral disc and the overall structure, function, and assembly of the ventral disc are not well understood. Our recent proteomic analysis of the ventral disc indicated that the median body protein (MBP), previously reported to localize exclusively to the median body, was primarily localized to the ventral disc. Using high-resolution light and electron microscopy, we confirm that the median body protein localizes primarily to the overlap zone of the ventral disc. The MBP also occasionally localized to the median body during prophase. To define the contribution of MBP to the ventral disc structure, we depleted MBP using an anti-MBP morpholino. We found that the ventral disc was no longer able to form properly and that the disc structure often had an aberrant nondomed or flattened horseshoe conformation. The ability of attached anti-MBP morpholino-treated trophozoites to withstand shear forces and normal forces was significantly decreased. Most notably, the plasma membrane contacts with the surface, including those of the bare area, were defective after the anti-MBP knockdown. To our knowledge, this is the first ventral disc protein whose depletion directly alters ventral disc structure, confirming that the domed ventral disc conformation is important for robust attachment.
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.