Oiling the key hole.
Many bacteria have been found to interact with specialized domains, rich in cholesterol and sphingolipids, of the host plasma membrane, termed lipid rafts. The mechanisms that underlie this interaction are starting to be unravelled. In this issue, Hayward et al. show that early effector proteins secreted by type III secretion harbouring Gram-negative bacteria are in fact cholesterol-binding proteins. Combined with other recent findings, this work shows that multiple steps leading to infection by these bacteria depend on raft components: activation of secretion, binding, perforation of the host cell membrane and signalling to trigger bacterial engulfment.
Lafont
Frank
F
Department Microbiology and Molecular Medicine, University of Geneva, 1 rue Michel Servet, 1211 Geneva 4, Switzerland.
van der Goot
F Gisou
FG
D001419:Bacteria / Q000378:metabolism* / Q000472:pathogenicity*; D001426:Bacterial Proteins / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism*; D006090:Gram-Negative Bacteria / Q000378:metabolism / Q000472:pathogenicity; D021962:Membrane Microdomains / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism; D010196:Pancreatic Elastase; D015398:Signal Transduction
D001426:Bacterial Proteins; D002352:Carrier Proteins; D008565:Membrane Proteins; C094579:invasion protein B, Salmonella typhimurium; C087447:ipaB protein, Shigella; D010196:Pancreatic Elastase; C017130:cholesterol-binding protein