5C69: Crystal Structure Of Prefusion-stabilized Rsv F Variant Pr-dm

Citation:
Abstract
Respiratory syncytial virus (RSV) causes acute lower respiratory tract infections and is the leading cause of infant hospitalizations. Recently, a promising vaccine antigen based on the RSV fusion protein (RSV F) stabilized in the native prefusion conformation has been described. Here we report alternative strategies to arrest RSV F in the prefusion conformation based on the prevention of hinge movements in the first refolding region and the elimination of proteolytic exposure of the fusion peptide. A limited number of unique mutations are identified that stabilize the prefusion conformation of RSV F and dramatically increase expression levels. This highly stable prefusion RSV F elicits neutralizing antibodies in cotton rats and induces complete protection against viral challenge. Moreover, the structural and biochemical analysis of the prefusion variants suggests a function for p27, the excised segment that precedes the fusion peptide in the polypeptide chain.
PDB ID: 5C69Download
MMDB ID: 132943
PDB Deposition Date: 2015/6/22
Updated in MMDB: 2015/09
Experimental Method:
x-ray diffraction
Resolution: 2.3  Å
Similar Structures:
Biological Unit for 5C69: hexameric; determined by author and by software (PISA)
Molecular Components in 5C69
Label Count Molecule
Proteins (6 molecules)
6
Fusion Glycoprotein F0,fibritin
Molecule annotation
Chemicals (83 molecules)
1
42
2
12
3
29
* Click molecule labels to explore molecular sequence information.

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