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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Authors: | D E Magoffin K Halpin P A Rota L-F Wang |
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Institution: | (1) CSIRO Livestock Industries, Australian Animal Health Laboratory, Geelong, Vic, Australia;(2) Curtin University of Technology, Perth, WA, Australia;(3) Centers for Disease Control and Prevention, Atlanta, GA, U.S.A. |
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Abstract: | 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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