000133573 001__ 133573
000133573 005__ 20180913055059.0
000133573 037__ $$aARTICLE
000133573 245__ $$aOiling the key hole
000133573 269__ $$a2005
000133573 260__ $$c2005
000133573 336__ $$aReviews
000133573 500__ $$aAuthor address: Department Microbiology and Molecular Medicine, University of Geneva, 1 rue Michel Servet, 1211 Geneva 4, Switzerland
000133573 520__ $$aMany bacteria have been found to interact with specialized domains, rich in cholesterol and sphingolipids, of the host plasma membrane, termed lipid rafts. The mechanisms that underlie this interaction are starting to be unravelled. In this issue, Hayward et al. show that early effector proteins secreted by type III secretion harbouring Gram-negative bacteria are in fact cholesterol-binding proteins. Combined with other recent findings, this work shows that multiple steps leading to infection by these bacteria depend on raft components: activation of secretion, binding, perforation of the host cell membrane and signalling to trigger bacterial engulfment
000133573 700__ $$aLafont, F.
000133573 700__ $$0240085$$avan der Goot, F. G.$$g171549
000133573 773__ $$j56$$k3$$q575-7$$tMol Microbiol
000133573 909C0 $$0252037$$pVDG$$xU11271
000133573 909CO $$ooai:infoscience.tind.io:133573$$pSV$$preview
000133573 937__ $$aVDG-REVIEW-2009-012
000133573 973__ $$aOTHER$$rREVIEWED$$sPUBLISHED
000133573 980__ $$aREVIEW