ArticleInfection and immunity2013
Vesicle-associated membrane protein 4 and syntaxin 6 interactions at the chlamydial inclusion.
Article in Infection and immunity, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Molecular and spatial integration of algal endosymbionts of the freshwater sponge, Ephydatia muelleri, throughout development in light and dark conditions.BMC genomics · 2026Article
- Review
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- Hijacking host cell vesicular transport: New insights into the nutrient acquisition mechanism ofVirulence · 2024Review
- Eukaryotic Clathrin Adapter Protein and Mediator of Cholesterol Homeostasis, PICALM, Affects Trafficking to the Chlamydial Inclusion.Molecular and cellular biology · 2023Article
- Shifting proteomes: limitations in using the BioID proximity labeling system to study SNARE protein trafficking during infection with intracellular pathogens.Pathogens and disease · 2021Article
- Got mutants? How advances in chlamydial genetics have furthered the study of effector proteins.Pathogens and disease · 2021Review
- Eukaryotic SNARE VAMP3 Dynamically Interacts with Multiple Chlamydial Inclusion Membrane Proteins.Infection and immunity · 2021Article
- Characterization of a monoacylglycerol lipase in the medicinal leech, Hirudo verbana.Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology · 2020Article
- Depletion of SNAP-23 and Syntaxin 4 alters lipid droplet homeostasis duringMicrobial cell (Graz, Austria) · 2019Article
- Proximity Labeling To Map Host-Pathogen Interactions at the Membrane of a Bacterium-Containing Vacuole in Chlamydia trachomatis-Infected Human Cells.Infection and immunity · 2019Article
- Functional inhibition of acid sphingomyelinase disrupts infection by intracellular bacterial pathogens.Life science alliance · 2019Article
- Chlamydial Infection From Outside to Inside.Frontiers in microbiology · 2019Review
- Development of a Proximity Labeling System to Map theFrontiers in cellular and infection microbiology · 2017Article
- Article
- Chlamydia cell biology and pathogenesis.Nature reviews. Microbiology · 2016Review
- The Proteome of the Isolated Chlamydia trachomatis Containing Vacuole Reveals a Complex Trafficking Platform Enriched for Retromer Components.PLoS pathogens · 2015Article
- The trans-Golgi SNARE syntaxin 10 is required for optimal development of Chlamydia trachomatis.Frontiers in cellular and infection microbiology · 2015Article
- Reconceptualizing the chlamydial inclusion as a pathogen-specified parasitic organelle: an expanded role for Inc proteins.Frontiers in cellular and infection microbiology · 2014Article
- The eukaryotic signal sequence, YGRL, targets the chlamydial inclusion.Frontiers in cellular and infection microbiology · 2014Article
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Authors and funding
5 authors.
Funding
Abstract
The predominant players in membrane fusion events are the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) family of proteins. We hypothesize that SNARE proteins mediate fusion events at the chlamydial inclusion and are important for chlamydial lipid acquisition. We have previously demonstrated that trans-Golgi SNARE syntaxin 6 localizes to the chlamydial inclusion. To investigate the role of syntaxin 6 at the chlamydial inclusion, we examined the localization and function of another trans-Golgi SNARE and syntaxin 6-binding partner, vesicle-associated membrane protein 4 (VAMP4), at the chlamydial inclusion. In this study, we demonstrate that syntaxin 6 and VAMP4 colocalize to the chlamydial inclusion and interact at the chlamydial inclusion. Furthermore, in the absence of VAMP4, syntaxin 6 is not retained at the chlamydial inclusion. Small interfering RNA (siRNA) knockdown of VAMP4 inhibited chlamydial sphingomyelin acquisition, correlating with a log decrease in infectious progeny. VAMP4 retention at the inclusion was shown to be dependent on de novo chlamydial protein synthesis, but unlike syntaxin 6, VAMP4 recruitment is observed in a species-dependent manner. Notably, VAMP4 knockdown inhibits sphingomyelin trafficking only to inclusions in which it localizes. These data support the hypothesis that VAMP proteins play a central role in mediating eukaryotic vesicular interactions at the chlamydial inclusion and, thus, support chlamydial lipid acquisition and chlamydial development.
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