Abstract
A truncated tagged form of the Autographica californica multiple nuclear polyhedrosis virus major surface glycoprotein, gp64, has been expressed using the baculovirus expression system and purified to homogeneity by immune-affinity chromatography. The protein, which is responsible for virus-cell fusion, was a trimer in solution and retained this oligomeric form at pH 5, the pH of fusion. Circular dichroism spectroscopy indicated a protein with mixed alpha-helix and beta-sheet content that did not undergo significant change at pH 5. The soluble protein showed no detectable binding to the insect cell surface. These data suggest a novel fusion mechanism for gp64 compared to models such as the influenza HA. In a crystal screen, deglycosylated, but not glycosylated, preparations of the protein were found to form small needle-shaped crystals that may form the basis of a dedicated structural study.
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