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2017 ; 8
(1
): 532
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A systematic exploration of the interactions between bacterial effector proteins
and host cell membranes
#MMPMID28912547
Weigele BA
; Orchard RC
; Jimenez A
; Cox GW
; Alto NM
Nat Commun
2017[Sep]; 8
(1
): 532
PMID28912547
show ga
Membrane-bound organelles serve as platforms for the assembly of multi-protein
complexes that function as hubs of signal transduction in eukaryotic cells.
Microbial pathogens have evolved virulence factors that reprogram these host
signaling responses, but the underlying molecular mechanisms are poorly
understood. Here we test the ability of ~200 type III and type IV effector
proteins from six Gram-negative bacterial species to interact with the eukaryotic
plasma membrane and intracellular organelles. We show that over 30% of the
effectors localize to yeast and mammalian cell membranes, including a subset of
previously uncharacterized Legionella effectors that appear to be able to
regulate yeast vacuolar fusion. A combined genetic, cellular, and biochemical
approach supports that some of the tested bacterial effectors can bind to
membrane phospholipids and may regulate membrane trafficking. Finally, we show
that the type III effector IpgB1 from Shigella flexneri may bind to acidic
phospholipids and regulate actin filament dynamics.Microbial pathogens secrete
effector proteins into host cells to affect cellular functions. Here, the authors
use a yeast-based screen to study around 200 effectors from six bacterial
species, showing that over 30% of them interact with the eukaryotic plasma
membrane or intracellular organelles.