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Effects of single amino acid substitutions at the E residue in the conserved GDNE motif of the Nipah virus polymerase (L) protein

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Summary

Nipah virus (NiV) is an emergent zoonotic paramyxovirus. The L proteins of most paramyxoviruses contain a GDNQ motif, thought to be part of the catalytic site for polymerase activity. Conversely, NiV L has GDNE in this position. We substituted the E residue with eight different amino acid residues and examined the effect on L function in an in vitro replication assay. Our results demonstrated that NiV L functioned with similar efficiency with either GDNE or GDNQ, but polymerase activity was severely reduced or abolished when a structurally destabilising residue (such as K, P or G) was introduced at this site.

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Authors and Affiliations

  1. CSIRO Livestock Industries, Australian Animal Health Laboratory, Geelong, Vic, Australia

    D. E. Magoffin, K. Halpin & L.-F. Wang

  2. Curtin University of Technology, Perth, WA, Australia

    D. E. Magoffin

  3. Centers for Disease Control and Prevention, Atlanta, GA, U.S.A.

    K. Halpin & P. A. Rota

Authors
  1. D. E. Magoffin
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  2. K. Halpin
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  3. P. A. Rota
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  4. L.-F. Wang
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Magoffin, D., Halpin, K., Rota, P. et al. Effects of single amino acid substitutions at the E residue in the conserved GDNE motif of the Nipah virus polymerase (L) protein. Arch Virol 152, 827–832 (2007). https://doi.org/10.1007/s00705-006-0881-1

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  • DOI: https://doi.org/10.1007/s00705-006-0881-1

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