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Hendra and Nipah virus W proteins with importin α

How two deadly bat-borne viruses hijack the machinery that carries proteins into the cell nucleus.

Importin α3 (pale gold surface) with the Hendra virus W peptide (plum) lying in its groove.

Hendra and Nipah are bat-borne viruses that are often fatal in people and animals. Their W proteins get into the cell nucleus by hitching a ride on importin α, the cell’s own nuclear import machinery, where they help switch off the immune response. These structures (6BW9 at 1.6 Å, with Nipah in 6BVV) show why the W proteins prefer importin α3: a larger contact surface and more than 50-fold tighter binding than with importin α1, set by the position of two of importin’s armadillo repeats.

This was a PhD project with Jade Forwood’s group at Charles Sturt University that I co-supervised, collecting data at the Australian Synchrotron and working through structure determination and refinement with the students (paper). I explained it on Portuguese radio as a book being smuggled into a house’s library (90 Segundos de Ciência).

PDB entry
6BW9 at PDBe (also at RCSB PDB)
Released
2018-07-04
Resolution
1.6 Å
Paper
Structural basis for importin alpha 3 specificity of W proteins in Hendra and Nipah viruses. (Nat Commun, 2018)
More
Technical details, links and electron density

Pictures and video rendered with UCSF ChimeraX; the 3D view is PDBe Mol*.

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