Detail
Článek
Článek online
FT
Medvik - BMČ
  • Je něco špatně v tomto záznamu ?

Soluble NSF attachment protein receptor molecular mimicry by a Legionella pneumophila Dot/Icm effector

NP. King, P. Newton, R. Schuelein, DL. Brown, M. Petru, V. Zarsky, P. Dolezal, L. Luo, A. Bugarcic, AC. Stanley, RZ. Murray, BM. Collins, RD. Teasdale, EL. Hartland, JL. Stow,

. 2015 ; 17 (6) : 767-84. [pub] 20150124

Jazyk angličtina Země Anglie, Velká Británie

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc16010668

Upon infection, Legionella pneumophila uses the Dot/Icm type IV secretion system to translocate effector proteins from the Legionella-containing vacuole (LCV) into the host cell cytoplasm. The effectors target a wide array of host cellular processes that aid LCV biogenesis, including the manipulation of membrane trafficking. In this study, we used a hidden Markov model screen to identify two novel, non-eukaryotic soluble NSF attachment protein receptor (SNARE) homologs: the bacterial Legionella SNARE effector A (LseA) and viral SNARE homolog A proteins. We characterized LseA as a Dot/Icm effector of L. pneumophila, which has close homology to the Qc-SNARE subfamily. The lseA gene was present in multiple sequenced L. pneumophila strains including Corby and was well distributed among L. pneumophila clinical and environmental isolates. Employing a variety of biochemical, cell biological and microbiological techniques, we found that farnesylated LseA localized to membranes associated with the Golgi complex in mammalian cells and LseA interacted with a subset of Qa-, Qb- and R-SNAREs in host cells. Our results suggested that LseA acts as a SNARE protein and has the potential to regulate or mediate membrane fusion events in Golgi-associated pathways.

Citace poskytuje Crossref.org

000      
00000naa a2200000 a 4500
001      
bmc16010668
003      
CZ-PrNML
005      
20160412124451.0
007      
ta
008      
160408s2015 enk f 000 0|eng||
009      
AR
024    7_
$a 10.1111/cmi.12405 $2 doi
024    7_
$a 10.1111/cmi.12405 $2 doi
035    __
$a (PubMed)25488819
040    __
$a ABA008 $b cze $d ABA008 $e AACR2
041    0_
$a eng
044    __
$a enk
100    1_
$a King, Nathan P $u Institute for Molecular Bioscience, The University of Queensland, Brisbane, Qld., Australia.
245    10
$a Soluble NSF attachment protein receptor molecular mimicry by a Legionella pneumophila Dot/Icm effector / $c NP. King, P. Newton, R. Schuelein, DL. Brown, M. Petru, V. Zarsky, P. Dolezal, L. Luo, A. Bugarcic, AC. Stanley, RZ. Murray, BM. Collins, RD. Teasdale, EL. Hartland, JL. Stow,
520    9_
$a Upon infection, Legionella pneumophila uses the Dot/Icm type IV secretion system to translocate effector proteins from the Legionella-containing vacuole (LCV) into the host cell cytoplasm. The effectors target a wide array of host cellular processes that aid LCV biogenesis, including the manipulation of membrane trafficking. In this study, we used a hidden Markov model screen to identify two novel, non-eukaryotic soluble NSF attachment protein receptor (SNARE) homologs: the bacterial Legionella SNARE effector A (LseA) and viral SNARE homolog A proteins. We characterized LseA as a Dot/Icm effector of L. pneumophila, which has close homology to the Qc-SNARE subfamily. The lseA gene was present in multiple sequenced L. pneumophila strains including Corby and was well distributed among L. pneumophila clinical and environmental isolates. Employing a variety of biochemical, cell biological and microbiological techniques, we found that farnesylated LseA localized to membranes associated with the Golgi complex in mammalian cells and LseA interacted with a subset of Qa-, Qb- and R-SNAREs in host cells. Our results suggested that LseA acts as a SNARE protein and has the potential to regulate or mediate membrane fusion events in Golgi-associated pathways.
650    _2
$a zvířata $7 D000818
650    _2
$a bakteriální proteiny $x metabolismus $7 D001426
650    _2
$a buněčné linie $7 D002460
650    _2
$a epitelové buňky $x mikrobiologie $7 D004847
650    12
$a interakce hostitele a patogenu $7 D054884
650    _2
$a lidé $7 D006801
650    _2
$a Legionella pneumophila $x fyziologie $7 D016952
650    _2
$a makrofágy $x mikrobiologie $7 D008264
650    _2
$a myši $7 D051379
650    12
$a molekulární mimikry $7 D018716
650    _2
$a sekvenční homologie aminokyselin $7 D017386
650    _2
$a rozpustné proteiny pro vazbu faktoru citlivého k N-ethylmaleimidu $x metabolismus $7 D052067
650    _2
$a faktory virulence $x metabolismus $7 D037521
655    _2
$a časopisecké články $7 D016428
655    _2
$a práce podpořená grantem $7 D013485
700    1_
$a Newton, Patrice $u Department of Microbiology and Immunology, University of Melbourne at the Peter Doherty Institute for Infection and Immunity, Melbourne, Vic., Australia.
700    1_
$a Schuelein, Ralf $u Department of Microbiology and Immunology, University of Melbourne at the Peter Doherty Institute for Infection and Immunity, Melbourne, Vic., Australia.
700    1_
$a Brown, Darren L $u Institute for Molecular Bioscience, The University of Queensland, Brisbane, Qld., Australia.
700    1_
$a Petru, Marketa $u Department of Parasitology, Charles University in Prague, Czech Republic.
700    1_
$a Zarsky, Vojtech $u Department of Parasitology, Charles University in Prague, Czech Republic.
700    1_
$a Dolezal, Pavel $u Department of Parasitology, Charles University in Prague, Czech Republic.
700    1_
$a Luo, Lin $u Institute for Molecular Bioscience, The University of Queensland, Brisbane, Qld., Australia.
700    1_
$a Bugarcic, Andrea $u Institute for Molecular Bioscience, The University of Queensland, Brisbane, Qld., Australia.
700    1_
$a Stanley, Amanda C $u Institute for Molecular Bioscience, The University of Queensland, Brisbane, Qld., Australia.
700    1_
$a Murray, Rachael Z $u Tissue Repair and Regeneration Program, Institute of Health and Biomedical Innovation, School of Biomedical Sciences, Faculty of Health, Queensland University of Technology, Brisbane, Qld., Australia.
700    1_
$a Collins, Brett M $u Institute for Molecular Bioscience, The University of Queensland, Brisbane, Qld., Australia.
700    1_
$a Teasdale, Rohan D $u Institute for Molecular Bioscience, The University of Queensland, Brisbane, Qld., Australia.
700    1_
$a Hartland, Elizabeth L $u Department of Microbiology and Immunology, University of Melbourne at the Peter Doherty Institute for Infection and Immunity, Melbourne, Vic., Australia.
700    1_
$a Stow, Jennifer L $u Institute for Molecular Bioscience, The University of Queensland, Brisbane, Qld., Australia.
773    0_
$w MED00007154 $t Cellular microbiology $x 1462-5822 $g Roč. 17, č. 6 (2015), s. 767-84
856    41
$u https://pubmed.ncbi.nlm.nih.gov/25488819 $y Pubmed
910    __
$a ABA008 $b sig $c sign $y a $z 0
990    __
$a 20160408 $b ABA008
991    __
$a 20160412124535 $b ABA008
999    __
$a ok $b bmc $g 1114097 $s 935036
BAS    __
$a 3
BAS    __
$a PreBMC
BMC    __
$a 2015 $b 17 $c 6 $d 767-84 $e 20150124 $i 1462-5822 $m Cellular microbiology $n Cell Microbiol $x MED00007154
LZP    __
$a Pubmed-20160408

Najít záznam

Citační ukazatele

Možnosti archivace