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Functional Analysis of the N-Linked Glycans Within the Fusion Protein of Respiratory Syncytial Virus

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Glycovirology Protocols

Part of the book series: Methods in Molecular Biology ((MIMB,volume 379))

Abstract

The respiratory syncytial virus fusion (F) protein is initially expressed as a single polypeptide chain (F0). The F0 subsequently undergoes posttranslational cleavage-by-cell protease activity to produce the F1 and F2 subunits. Each of the two subunits within the mature F protein is modified by the addition of N-linked glycans. The individual N-linked glycans on the F protein were selectively removed by using site-directed mutagenesis to mutate the individual glycan-acceptor sites. In this way the role of these individual glycans in targeting of the F protein to the cell surface, and on the ability of the F protein to induce membrane fusion, was examined.

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© 2007 Humana Press Inc., Totowa, NJ

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Li, P., Rixon, H.W.M., Brown, G., Sugrue, R.J. (2007). Functional Analysis of the N-Linked Glycans Within the Fusion Protein of Respiratory Syncytial Virus. In: Sugrue, R.J. (eds) Glycovirology Protocols. Methods in Molecular Biology, vol 379. Humana Press. https://doi.org/10.1007/978-1-59745-393-6_5

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  • DOI: https://doi.org/10.1007/978-1-59745-393-6_5

  • Publisher Name: Humana Press

  • Print ISBN: 978-1-58829-590-3

  • Online ISBN: 978-1-59745-393-6

  • eBook Packages: Springer Protocols

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