Chlamydia trachomatis interrupts an exocytic pathway to acquire endogenously synthesized sphingomyelin in transit from the Golgi apparatus to the plasma membrane.

TitleChlamydia trachomatis interrupts an exocytic pathway to acquire endogenously synthesized sphingomyelin in transit from the Golgi apparatus to the plasma membrane.
Publication TypeJournal Article
Year of Publication1996
AuthorsHackstadt T, Rockey DD, Heinzen RA, Scidmore MA
JournalThe EMBO journal
Volume15
Issue5
Pagination964-77
Date Published1996 Mar 1
ISSN0261-4189
Keywords4-Chloro-7-nitrobenzofurazan, Animals, Anti-Bacterial Agents, Biological Transport, Active, Brefeldin A, Cell Membrane, Ceramides, Chlamydia Infections, Chlamydia trachomatis, Cyclopentanes, Exocytosis, Fluorescent Dyes, Golgi Apparatus, Hela Cells, Humans, Inclusion Bodies, Macrolides, Membrane Fusion, Microscopy, Electron, Models, Biological, Sphingomyelins
Abstract

Chlamydia trachomatis acquires C6-NBD-sphingomyelin endogenously synthesized from C6-NBD-ceramide and transported to the vesicle (inclusion) in which they multiply. Here we explore the mechanisms of this unusual trafficking and further characterize the association of the chlamydial inclusion with the Golgi apparatus. Endocytosed chlamydiae are trafficked to the Golgi region and begin to acquire sphingolipids from the host within a few hours following infection. The transport of NBD-sphingolipid to the inclusion is energy- and temperature-dependent with the characteristics of an active, vesicle-mediated process. Photo-oxidation of C5-DMB-ceramide, in the presence of diaminobenzidine, identified DMB-lipids in vesicles in the process of fusing to the chlamydial inclusion membrane. C6-NBD-sphingomyelin incorporated into the plasma membrane is not trafficked to the inclusion to a significant degree, suggesting the pathway for sphingomyelin trafficking is direct from the Golgi apparatus to the chlamydial inclusion. Lectins and antibody probes for Golgi-specific glycoproteins demonstrate the close association of the chlamydial inclusion with the Golgi apparatus but do not detect these markers in the inclusion membrane. Collectively, the data are consistent with a model in which C.trachomatis inhabits a unique vesicle which interrupts an exocytic pathway to intercept host sphingolipids in transit from the Golgi apparatus to the plasma membrane.

Alternate JournalEMBO J.