title: Membrane contact sites between pathogen-containing compartments and host organelles.
abstract: Intracellular pathogens survive and replicate within specialised membrane-bound compartments that can be considered as pseudo-organelles. Using the obligate intracellular bacterium Chlamydia as an illustrative example, we consider the modes of lipid transport between pathogen-containing compartments and host organelles, including the formation of static membrane contact sites. We discuss how lipid scavenging can be mediated via the reprogramming of cellular transporters at these interfaces and describe recent data suggesting that pathogen effectors modulate the formation of specific membrane contacts. Further study of these emerging mechanisms is likely to yield new insights into the cell biology of lipid transport and organelle communication, which highlights potential new targets and strategies for future therapeutics. This article is part of a Special Issue entitled: The cellular lipid landscape edited by Tim P. Levine and Anant K. Menon.
authors.affiliation: Institute of Structural and Molecular Biology, University College London & Birkbeck, Malet Street, London WC1E 7HX, UK.
authors.forename: Maud
authors.initials: M
authors.lastname: Dumoux
authors.affiliation: Institute of Structural and Molecular Biology, University College London & Birkbeck, Malet Street, London WC1E 7HX, UK. Electronic address: richard.hayward@ucl.ac.uk.
authors.forename: Richard D
authors.initials: RD
authors.lastname: Hayward
mesh_terms: D000818:Animals; D001692:Biological Transport; D002462:Cell Membrane / Q000378:metabolism*; D002689:Chlamydia / Q000378:metabolism*; D006056:Golgi Apparatus / Q000378:metabolism; D054884:Host-Pathogen Interactions / Q000502:physiology*; D006801:Humans; D002479:Inclusion Bodies / Q000378:metabolism* / Q000382:microbiology; D015388:Organelles / Q000378:metabolism*; D013109:Sphingomyelins / Q000378:metabolism
chemical_list: D013109:Sphingomyelins
keywords: Lipid; Membrane contact; Organelle; Pathogen; Type III secretion