Structure of the primed paramyxovirus fusion protein

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Structure of the primed paramyxovirus fusion protein.

V iruses with lipid envelopes must fuse their membranes with those of host cells to transfer their genomes and initiate infection. Depending on the virus, the membrane fusion process can occur at the plasma membrane, or at intracellular membranes following the internalization of virus particles. Not surprisingly, the viral proteins responsible for membrane fusion are highly diverse, as are the ...

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Class I viral fusion proteins share common mechanistic and structural features but little sequence similarity. Structural insights into the protein conformational changes associated with membrane fusion are based largely on studies of the influenza virus hemagglutinin in pre- and postfusion conformations. Here, we present the crystal structure of the secreted, uncleaved ectodomain of the paramy...

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Oral 1 STRUCTURE AND ACTIVATION OF PARAMYXOVIRUS FUSION GLYCOPROTEINS

Fusion of the lipid envelope of paramyxoviruses with the host cell plasma membrane during virus entry is mediated by the F protein, a trimeric extracellular transmembrane-anchored glycoprotein. During F-mediated fusion, its fusion peptide inserts into the host cell membrane, followed by large-scale refolding from a largely globular pre-fusion conformation to a golf tee-shaped postfusion conform...

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Mutations in multiple domains activate paramyxovirus F protein-induced fusion.

SER virus, a paramyxovirus that is closely related to simian virus 5 (SV5), is unusual in that it fails to induce syncytium formation. The SER virus F protein has an unusually long cytoplasmic tail (CT), and it was previously observed that truncations or specific mutations of this domain result in enhanced syncytium formation. In addition to the long CT, the SER F protein has nine amino acid di...

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ژورنال

عنوان ژورنال: Proceedings of the National Academy of Sciences

سال: 2012

ISSN: 0027-8424,1091-6490

DOI: 10.1073/pnas.1214903109