Negative charge and membrane-tethered viral 3B cooperate to recruit viral RNA dependent RNA polymerase 3D(pol)
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F17%3A00483897" target="_blank" >RIV/61388963:_____/17:00483897 - isvavai.cz</a>
Result on the web
<a href="https://www.nature.com/articles/s41598-017-17621-6" target="_blank" >https://www.nature.com/articles/s41598-017-17621-6</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/s41598-017-17621-6" target="_blank" >10.1038/s41598-017-17621-6</a>
Alternative languages
Result language
angličtina
Original language name
Negative charge and membrane-tethered viral 3B cooperate to recruit viral RNA dependent RNA polymerase 3D(pol)
Original language description
Most single stranded plus RNA viruses hijack phosphatidylinositol 4-kinases (PI4Ks) to generate membranes highly enriched in phosphatidylinositol 4-phosphate (PI4P). These membranous compartments known as webs, replication factories or replication organelles are essential for viral replication because they provide protection from the innate intracellular immune response while serving as platforms for viral replication. Using purified recombinant proteins and biomimetic model membranes we show that the nonstructural viral 3A protein is sufficient to promote membrane hyper-phosphorylation given the proper intracellular cofactors (PI4KB and ACBD3). However, our bio-mimetic in vitro reconstitution assay revealed that rather than the presence of PI4P specifically, negative charge alone is sufficient for the recruitment of 3D(pol) enzymes to the surface of the lipid bilayer. Additionally, we show that membrane tethered viral 3B protein (also known as Vpg) works in combination with the negative charge to increase the efficiency of membrane recruitment of 3D(pol).
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
<a href="/en/project/GJ15-21030Y" target="_blank" >GJ15-21030Y: In vitro reconstitution of viral “Replication factories“</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2017
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Scientific Reports
ISSN
2045-2322
e-ISSN
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Volume of the periodical
7
Issue of the periodical within the volume
Dec 11
Country of publishing house
GB - UNITED KINGDOM
Number of pages
11
Pages from-to
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UT code for WoS article
000417570500028
EID of the result in the Scopus database
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