Two heptad-repeat regions (HR1 and HR2) are highly conserved in paramyxovirus fusion proteins and form a stable helical trimer of heterodimers [(HR1-HR2)(3)] after the fusion between viral and cellular membranes. In t...
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Two heptad-repeat regions (HR1 and HR2) are highly conserved in paramyxovirus fusion proteins and form a stable helical trimer of heterodimers [(HR1-HR2)(3)] after the fusion between viral and cellular membranes. In this study, two HR regions of the fusion protein of measles virus, a member of the paramyxoviruses, were selected and overexpressed as a single chain (named 2-Helix) connected by an amino-acid linker using a GST-fusion expression system in Escherichia coli. Crystals of 2-Helix protein (GST removed) could be obtained from many conditions using the sitting- or hanging-drop vapour-diffusion method. A complete data set was collected in-house to 1.9 Angstrom resolution from a single crystal. The crystal belongs to space group P6, with unit-cell parameters a = b = 51.637, c = 67.058 Angstrom. To facilitate the crystal structure solution, SeMet-substituted 2-Helix crystals, grown under similar conditions to the native, were also obtained and diffracted X-rays to 1.8 Angstrom using synchrotron radiation.
The fusion glycoprotein (F protein) of paramyxoviruses plays a vital role in virus-induced cytopathology. To explore the role of the F protein in peste des petits ruminants virus (PPRV)-induced cytopathology, the F pr...
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The fusion glycoprotein (F protein) of paramyxoviruses plays a vital role in virus-induced cytopathology. To explore the role of the F protein in peste des petits ruminants virus (PPRV)-induced cytopathology, the F protein of PPRV was purified by immunoaffinity chromatography. The purified F protein, when incubated with chicken erythrocytes, caused lysis suggesting that PPRV F protein is a hemolysin. Furthermore, the hemolysis can be inhibited by hyperimmune serum against F protein. The virus-induced cell fusion (syncytia) was also inhibited by the hyperimmune serum against the F protein. In summary, these results indicate that the purified PPRV F protein is biologically active and is involved in virus-induced hemolysis, cell-fusion and the initiation of infection.
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