Zobrazeno 1 - 10
of 23
pro vyhledávání: '"David Chetrit"'
Autor:
Silke Malmsheimer, Iwan Grin, Erwin Bohn, Mirita Franz-Wachtel, Boris Macek, Tobias Sahr, Fabian Smollich, David Chetrit, Amit Meir, Craig Roy, Carmen Buchrieser, Samuel Wagner
Publikováno v:
PLoS Pathogens, Vol 20, Iss 11, p e1012118 (2024)
To promote intracellular survival and infection, Legionella spp. translocate hundreds of effector proteins into eukaryotic host cells using a type IV b protein secretion system (T4bSS). T4bSS are well known to translocate soluble as well as transmemb
Externí odkaz:
https://doaj.org/article/4d14b00b8b904a6ab57bd36d6767e7d9
Autor:
Amit Meir, Kevin Macé, Natalya Lukoyanova, David Chetrit, Manuela K. Hospenthal, Adam Redzej, Craig Roy, Gabriel Waksman
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
A membrane-embedded complex (called T4CC) is essential for injection of Legionella pneumophila effector proteins into human macrophages via a Type IV secretion system. Here, the authors purify and study the T4CC using functional and cryo-EM structura
Externí odkaz:
https://doaj.org/article/1f01a2ef3e6d4f6f8a81da89f176c9c9
Publikováno v:
mBio, Vol 11, Iss 1 (2020)
ABSTRACT Type IV secretion systems (T4SSs) are sophisticated nanomachines used by many bacterial pathogens to translocate protein and DNA substrates across a host cell membrane. Although T4SSs have important roles in promoting bacterial infections, l
Externí odkaz:
https://doaj.org/article/7e1bcf1f2afc42b7b966cb330d2a0118
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
Legionella pneumophila employs the Type 4B secretion system (T4BSS) to translocate more than 300 effector proteins into the host cell during infection. Here the authors present the crystal structure of the DotM soluble domain and give mechanistic ins
Externí odkaz:
https://doaj.org/article/6c642b7b193d45158274212a71865767
Publikováno v:
PLoS Pathogens, Vol 8, Iss 11, p e1002988 (2012)
The intracellular pathogen Legionella pneumophila translocates a large number of effector proteins into host cells via the Icm/Dot type-IVB secretion system. Some of these effectors were shown to cause lethal effect on yeast growth. Here we character
Externí odkaz:
https://doaj.org/article/bb38850f113d467ab5baee0cafbe8ba1
Autor:
Yuval Cabilly, Mali Barbi, Michal Geva, Liraz Marom, David Chetrit, Marcelo Ehrlich, Orna Elroy-Stein
Publikováno v:
PLoS ONE, Vol 7, Iss 10, p e46715 (2012)
BACKGROUND: Mutations in any of the five subunits of eukaryotic translation initiation factor 2B (eIF2B) can lead to an inherited chronic-progressive fatal brain disease of unknown aetiology termed leucoencephalopathy with vanishing white matter (VWM
Externí odkaz:
https://doaj.org/article/8e80a7d06970427b858acc4357570e71
Autor:
Natalya Lukoyanova, Kevin Macé, Craig R. Roy, David Chetrit, Gabriel Waksman, Adam Redzej, Amit Meir, Manuela K. Hospenthal
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
Nature Communications, 11 (1)
Nature Communications
Nature Communications, 11 (1)
Nature Communications
Legionella pneumophila is a bacterial pathogen that utilises a Type IV secretion (T4S) system to inject effector proteins into human macrophages. Essential to the recruitment and delivery of effectors to the T4S machinery is the membrane-embedded T4
Publikováno v:
Journal of visualized experiments : JoVE. (157)
The Dot/Icm secretion system of Legionella pneumophila is a complex type IV secretion system (T4SS) nanomachine that localizes at the bacterial pole and mediates the delivery of protein and DNA substrates to target cells, a process generally requirin
Publikováno v:
Journal of Visualized Experiments.
The Dot/Icm secretion system of Legionella pneumophila is a complex type IV secretion system (T4SS) nanomachine that localizes at the bacterial pole and mediates the delivery of protein and DNA substrates to target cells, a process generally requirin
Publikováno v:
Nature microbiology
Type IV secretion systems (T4SSs) are complex machines used by bacteria to deliver protein and DNA complexes into target host cells1–5. Conserved ATPases are essential for T4SS function, but how they coordinate their activities to promote substrate