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Negative charge and membrane-tethered viral 3B cooperate to recruit viral RNA dependent RNA polymerase 3D pol
A. Dubankova, J. Humpolickova, M. Klima, E. Boura,
Language English Country England, Great Britain
Document type Journal Article, Research Support, Non-U.S. Gov't
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- MeSH
- Adaptor Proteins, Signal Transducing genetics metabolism MeSH
- Cell Membrane metabolism MeSH
- Phosphatidylinositol Phosphates metabolism MeSH
- Phosphotransferases (Alcohol Group Acceptor) genetics metabolism MeSH
- Kobuvirus enzymology MeSH
- Humans MeSH
- Membrane Proteins genetics metabolism MeSH
- Picornaviridae Infections metabolism virology MeSH
- Viral Nonstructural Proteins genetics metabolism MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
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 3Dpol 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 3Dpol.
References provided by Crossref.org
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