What is the clinical evidence from this study?

Study design: Other. Population: Cardiovirus infection. Intervention: Mengovirus Leader protein (LM). Primary outcome: NMR solution structures of LM, its phosphorylated derivatives, and Ran:LM0P complex.

October 20, 2014Proceedings of the National Academy of Sciences

Solution structures of Mengovirus Leader protein, its phosphorylated derivatives, and in complex with nuclear transport regulatory protein, RanGTPase

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Key result

NMR structures of the Mengovirus Leader protein in complex with RanGTPase reveal it binds the RanBP1 site, exposing its zinc finger and phosphorylation sites to potentially recruit exportins.

Population

Recombinant Mengovirus Leader protein and RanGTPase protein

Comparison

Phosphorylation of LM protein and complex… vs Unphosphorylated LM protein and unbound RanGTPase

Design

Preclinical

Authors

VBValjean Raiden Bacot-DavisStony Brook Medicine JCJessica J. Ciomperlik HBHolly A. Basta

Discussion

Member takes

Implication

Structural details of viral RanBP1 mimicry identified; leaves open relevance to cardiovirus myocarditis or antiviral targeting.

Structured PICO

Population

Recombinant Mengovirus Leader (LM) protein (unphosphorylated, singly phosphorylated, doubly phosphorylated) and RanGTPase protein

Intervention

Phosphorylation of LM protein and complex formation with RanGTPase

Comparator

Unphosphorylated LM protein and unbound RanGTPase

Outcome

Solution structures determined by NMR spectroscopysurrogate

The NMR structures of Mengovirus Leader protein and its complex with RanGTPase reveal the structural basis for how the viral protein perverts host nucleocytoplasmic trafficking.

Limitations

The model of the Ran:LM:Crm1 ternary complex is speculative and requires further experimental validation.

Cite This Study

Bacot‐Davis et al. (2014) studied Cardiovirus infection. Mengovirus Leader protein (LM) was evaluated on NMR solution structures of LM, its phosphorylated derivatives, and Ran:LM0P complex. NMR structures of the Mengovirus Leader protein in complex with RanGTPase reveal it binds the RanBP1 site, exposing its zinc finger and phosphorylation sites to potentially recruit exportins.

synapsesocial.com/papers/6a89745a81d3bfa98ef7cb32 https://doi.org/10.1073/pnas.1411098111

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Solution structures of Mengovirus Leader protein, its phosphorylated derivatives, and in complex with nuclear transport regulatory protein, RanGTPase

Discussion

Member takes

Implication

Structured PICO

Limitations

Cite This Study

Solution structures of Mengovirus Leader protein, its phosphorylated derivatives, and in complex with nuclear transport regulatory protein, RanGTPase

Discussion

Member takes

Implication

Structured PICO

Limitations

Cite This Study

Also Consider

Also Consider