Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
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Target Concepts:
Gene/Protein
Disease
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Enzyme
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Query: UMLS:C0023241 (
Legionella
)
6,990
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Incubation of
Legionella
pneumophila Philadelphia 1 in normal human serum depleted of either classical-pathway component C1q or alternative-pathway component
factor B
resulted in activation of the complement system. Experiments focused on the role of the classical pathway in complement activation revealed that legionellae bound C1q independently of antibody. Purified preparations of L. pneumophila major outer membrane protein but not serogroup 1 lipopolysaccharide bound C1q independently of antibody. This suggests that antibody-independent binding of C1q by L. pneumophila can result in activation of the classical pathway in normal human serum and that major outer membrane protein may be a C1q acceptor on the L. pneumophila cell surface.
...
PMID:Antibody-independent binding of complement component C1q by Legionella pneumophila. 759 Nov 61
Legionella
pneumophila, the Gram-negative pathogen causing
Legionnaires' disease
, infects host cells by hijacking endocytic pathways and forming a
Legionella
-containing vacuole (LCV) in which the bacteria replicate. To promote LCV expansion and prevent lysosomal targeting, effector proteins are translocated into the host cell where they alter membrane traffic. Here we show that three of these effectors [LegC2 (
Legionella
eukaryotic-like gene C2)/YlfB (yeast lethal
factor B
), LegC3, and LegC7/YlfA] functionally mimic glutamine (Q)-SNARE proteins. In infected cells, the three proteins selectively form complexes with the endosomal arginine (R)-SNARE vesicle-associated membrane protein 4 (VAMP4). When reconstituted in proteoliposomes, these proteins avidly fuse with liposomes containing VAMP4, resulting in a stable complex with properties resembling canonical SNARE complexes. Intriguingly, however, the LegC/SNARE hybrid complex cannot be disassembled by N-ethylmaleimide-sensitive factor. We conclude that LegCs use SNARE mimicry to divert VAMP4-containing vesicles for fusion with the LCV, thus promoting its expansion. In addition, the LegC/VAMP4 complex avoids the host's disassembly machinery, thus effectively trapping VAMP4 in an inactive state.
...
PMID:Direct targeting of membrane fusion by SNARE mimicry: Convergent evolution of Legionella effectors. 2743 92