3J9F

Poliovirus complexed with soluble, deglycosylated poliovirus receptor (Pvr) at 4 degrees C

Summary for 3J9F

• Entry DOI: 10.2210/pdb3j9f/pdb
• EMDB information: 6242 6243
• Descriptor: Protein VP1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (13 entities in total)
• Functional Keywords: deglycosylated receptor, picornavirus, pvr, cd155, enterovirus, cell entry, virus-cell adhesion complex, virus/cell adhesion
• Biological source: Human poliovirus 1 Mahoney; More
• Total number of polymer chains: 7
• Total formula weight: 135663.47

Authors

Strauss, M.,Filman, D.J.,Belnap, D.M.,Cheng, N.,Noel, R.T.,Hogle, J.M. (deposition date: 2015-01-15, release date: 2015-02-11, Last modification date: 2022-12-21)

Primary citation

Strauss, M.,Filman, D.J.,Belnap, D.M.,Cheng, N.,Noel, R.T.,Hogle, J.M.
Nectin-Like Interactions between Poliovirus and Its Receptor Trigger Conformational Changes Associated with Cell Entry.
J.Virol., 89:4143-4157, 2015

PubMed Abstract: Poliovirus infection is initiated by attachment to a receptor on the cell surface called Pvr or CD155. At physiological temperatures, the receptor catalyzes an irreversible expansion of the virus to form an expanded form of the capsid called the 135S particle. This expansion results in the externalization of the myristoylated capsid protein VP4 and the N-terminal extension of the capsid protein VP1, both of which become inserted into the cell membrane. Structures of the expanded forms of poliovirus and of several related viruses have recently been reported. However, until now, it has been unclear how receptor binding triggers viral expansion at physiological temperature. Here, we report poliovirus in complex with an enzymatically partially deglycosylated form of the 3-domain ectodomain of Pvr at a 4-Å resolution, as determined by cryo-electron microscopy. The interaction of the receptor with the virus in this structure is reminiscent of the interactions of Pvr with its natural ligands. At a low temperature, the receptor induces very few changes in the structure of the virus, with the largest changes occurring within the footprint of the receptor, and in a loop of the internal protein VP4. Changes in the vicinity of the receptor include the displacement of a natural lipid ligand (called "pocket factor"), demonstrating that the loss of this ligand, alone, is not sufficient to induce particle expansion. Finally, analogies with naturally occurring ligand binding in the nectin family suggest which specific structural rearrangements in the virus-receptor complex could help to trigger the irreversible expansion of the capsid.

PubMed: 25631086
DOI: 10.1128/JVI.03101-14

Experimental method

ELECTRON MICROSCOPY (9 Å)