ArticleProceedings of the National Academy of Sciences of the United States of America2013
CCT chaperonin complex is required for efficient delivery of anthrax toxin into the cytosol of host cells.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Cryo-EM structure of the fully-loaded asymmetric anthrax lethal toxin in its heptameric pre-pore state.PLoS pathogens · 2020Article
- Effects of ricin on primary pulmonary alveolar macrophages.The Journal of international medical research · 2019Article
- The chaperonin TRiC/CCT is essential for the action of bacterial glycosylating protein toxins likeProceedings of the National Academy of Sciences of the United States of America · 2018Article
- The chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosol.Cellular microbiology · 2017Article
- Structure of anthrax lethal toxin prepore complex suggests a pathway for efficient cell entry.The Journal of general physiology · 2016Article
- Article
- A Heterologous Reporter Defines the Role of the Tetanus Toxin Interchain Disulfide in Light-Chain Translocation.Infection and immunity · 2015Article
- TCP1 complex proteins interact with phosphorothioate oligonucleotides and can co-localize in oligonucleotide-induced nuclear bodies in mammalian cells.Nucleic acids research · 2014Article
- Hijacking multivesicular bodies enables long-term and exosome-mediated long-distance action of anthrax toxin.Cell reports · 2013Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Bacterial toxins have evolved successful strategies for coopting host proteins to access the cytosol of host cells. Anthrax lethal factor (LF) enters the cytosol through pores in the endosomal membrane formed by anthrax protective antigen. Although in vitro models using planar lipid bilayers have shown that translocation can occur in the absence of cellular factors, recent studies using intact endosomes indicate that host factors are required for translocation in the cellular environment. In this study, we describe a high-throughput shRNA screen to identify host factors required for anthrax lethal toxin-induced cell death. The cytosolic chaperonin complex chaperonin containing t-complex protein 1 (CCT) was identified, and subsequent studies showed that CCT is required for efficient delivery of LF and related fusion proteins into the cytosol. We further show that knockdown of CCT inhibits the acid-induced delivery of LF and the fusion protein LFN-Bla (N terminal domain of LF fused to β-lactamase) across the plasma membrane of intact cells. Together, these results suggest that CCT is required for efficient delivery of enzymatically active toxin to the cytosol and are consistent with a direct role for CCT in translocation of LF through the protective antigen pore.
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