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Comment
. 2012 Oct 9;109(41):16404-5.
doi: 10.1073/pnas.1214903109. Epub 2012 Oct 1.

Structure of the primed paramyxovirus fusion protein

David A Steinhauer  1 , Richard Karl Plemper
Affiliations
Comment

Structure of the primed paramyxovirus fusion protein

David A Steinhauer et al. Proc Natl Acad Sci U S A. .
No abstract available

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Fig. 1.
Fig. 1.
Cartoon of type I VFP-mediated viral entry, represented by example of the paramyxovirus F protein. Upon synthesis, uncleaved F assumes a metastable prefusion conformation (Left). Proteolytic maturation generates the fusion-ready prefusion form of the trimer (center, Left). Receptor binding by the associated attachment glycoprotein triggers major conformational changes of the primed F protein trimer. Refolding is considered to occur through a series of temporary conformations, including a hypothetical prehairpin intermediate (center, Right). Ultimately, the F protein assumes a thermodynamically highly stable postfusion conformation in which transmembrane domains and fusion peptides, and thus viral envelope and target membrane, are posited in close proximity (Right). Opening of a fusion pore enabling viral entry most likely requires concerted refolding of multiple F protein complexes. Structural renderings are based on original crystal structures [uncleaved prefusion F protein, Protein Data Bank (PDB) accession no. 2B9B; cleaved prefusion F protein from Welsh et al. (8); postfusion F protein, PDB accession no. 1ZTM) or hypothetical structural models (F protein prehairpin intermediate).
Fig. 2.
Fig. 2.
Ribbon representations of immature and mature prefusion paramyxovirus F protein [Left, PDB accession no. 2B9B and Welsh et al. (8)] and influenza virus HA (Right, PDB accession nos. 1HA0 and 2IBX) protein trimers, colored by monomer. Residues immediately upstream to the cleavage sites are colored dark blue, whereas residues immediately downstream representing the N-terminal sections of the fusion peptides are shown in red. Numbers and arrows (Upper) specify residue upstream to the cleavage sites in one of the monomers. Upon proteolytic maturation, only minor relocation of the newly generated N- and C-termini are observed in paramyxovirus F protein, whereas the N-terminal region of the influenza virus HA fusion peptide inserts deeply into the trimer interior (arrows, Lower). Numbers represent distance between chain termini after cleavage.
See this image and copyright information in PMC

Comment on

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