Pre-fusion rsv f antigens
A pre-fusion, chimeric technology, applied in the direction of fusion peptides, viral antigen components, antiviral agents, etc., can solve the problem of not producing candidates
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[0535] 1. Post-fusion structure and pre-fusion model
[0536] RSV F structure after fusion
[0537] A stable, non-aggregating soluble RSV F subunit antigen ( figure 1 ). This engineered F is efficiently expressed and easily purified. Electron micrographs of negatively stained samples show the formation of non-aggregated, uniform cane-shaped molecules, consistent with postfused F trimers ( figure 2 A). The engineered F trimer is stable, and the circular dichroism spectrum shows no obvious melting when the temperature is up to 95 °C ( figure 2 B and 2C).
[0538] The RSV F protein was crystallized, and its structure was determined by molecular substitution and three-fold non-crystallographic symmetry (NCS) averaging (Table 3 and image 3 ). The structure does not include the p27 fragment (peptide between the two furin sites, which is lost after cleavage), the fusion peptide, the transmembrane region and the cytoplasmic domain ( Figure 4 ).
[0539] Table 3. Crysta...
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