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Evidence that the fusion protein of respiratory syncytial virus exists as a dimer in its native form

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Summary

The quarternary structure of respiratory syncytial virus (RSV) fusion protein has been studied. Crosslinking studies were done to stabilize the non-covalently associated proteins. These stable, heat-resistant, covalently linked complexes were analyzed by sodium dodecyl sulfate-polyacrylamide electrophoresis. In situ crosslinking studies demonstrated that the fusion protein of RSV exists as a dimer in its native form on the surface of infected cells. The purified protein was also found to be present predominantly as a dimer. In addition, the results suggest that F1 subunits may play a role in the dimerization of the fusion protein.

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Authors and Affiliations

  1. Praxis Biologics, Virology Research, Rochester, New York, USA

    R. G. Arumugham, S. W. Hildreth & P. R. Paradiso

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  1. R. G. Arumugham
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  2. S. W. Hildreth
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  3. P. R. Paradiso
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Arumugham, R.G., Hildreth, S.W. & Paradiso, P.R. Evidence that the fusion protein of respiratory syncytial virus exists as a dimer in its native form. Archives of Virology 106, 327–334 (1989). https://doi.org/10.1007/BF01313961

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  • DOI: https://doi.org/10.1007/BF01313961

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