ArticleBiochemical and biophysical research communications2018
Both the N- and C- terminal regions of the Chlamydial inclusion protein D (IncD) are required for interaction with the pleckstrin homology domain of the ceramide transport protein CERT.
Article in Biochemical and biophysical research communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 23 citations in OpenAlex.
- Inclusion Membrane Proteins ofMicroorganisms · 2026Review
- Pathogenicity and virulence ofVirulence · 2025Review
- Host sphingolipids supportmBio · 2025Article
- Endoplasmic reticulum: the target of chlamydial manipulation.Archives of microbiology · 2025Review
- Recruitment of the cellular lipid transport protein CERT to C. psittaci inclusions regulates the timing of bacterial egress.Scientific reports · 2025Article
- Inc/GFP chimera protein-based interactomics reveals host cellular interactions of Cps0558, a novel Chlamydia psittaci inclusion protein.Pathogens and disease · 2025Article
- Transmembrane substrates of type three secretion system injectisomes.Microbiology (Reading, England) · 2023Review
- Natural Ligand-Mimetic and Nonmimetic Inhibitors of the Ceramide Transport Protein CERT.International journal of molecular sciences · 2022Review
- VAP Proteins - From Organelle Tethers to Pathogenic Host Interactors and Their Role in Neuronal Disease.Frontiers in cell and developmental biology · 2022Review
- Ceramide Transfer Protein (CERT): An Overlooked Molecular Player in Cancer.International journal of molecular sciences · 2021Review
- Got mutants? How advances in chlamydial genetics have furthered the study of effector proteins.Pathogens and disease · 2021Review
- Functions of Sphingolipids in Pathogenesis During Host-Pathogen Interactions.Frontiers in microbiology · 2021Review
- The vacuole guard hypothesis: how intravacuolar pathogens fight to maintain the integrity of their beloved home.Current opinion in microbiology · 2020Review
- Sphingolipid Metabolism and Transport inFrontiers in cell and developmental biology · 2019Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Chlamydia trachomatis is an obligate intracellular bacterium that replicates within a membranous compartment, the inclusion, in host cells. Its intracellular life cycle requires host sphingolipids, which are in part acquired through the ER-Golgi localized ceramide transport protein (CERT). The Chlamydia-encoded inclusion membrane protein IncD is composed of two closely linked long hydrophobic domains with their N- and C-termini exposed to the host cytosol. IncD binds directly to the pleckstrin homology (PH) domain of CERT, likely redirecting ceramide to the inclusion. The precise regions of IncD required for this interaction have not been delineated. Using co-transfection studies together with phylogenetic studies, we demonstrate that both the IncD N- and C-terminal regions are required for binding to the CERT PH domain and define key interaction residues. Native gel electrophoresis analysis demonstrates that the transmembrane region of IncD forms SDS-resistant but dithiothreitol-sensitive homodimers, which in turn can assemble to form higher order oligomers through additional N- and C-terminal domain contacts. IncD oligomerization may facilitate high affinity binding to CERT, allowing C. trachomatis to efficiently redirect host ceramide to the inclusion.
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Registered trials
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