title: Effects of single amino acid substitutions at the E residue in the conserved GDNE motif of the Nipah virus polymerase (L) protein.
abstract: 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.
authors.affiliation: CSIRO Livestock Industries, Australian Animal Health Laboratory, Geelong, Vic, Australia.
authors.forename: D E
authors.initials: DE
authors.lastname: Magoffin
authors.forename: K
authors.initials: K
authors.lastname: Halpin
authors.forename: P A
authors.initials: PA
authors.lastname: Rota
authors.forename: L-F
authors.initials: LF
authors.lastname: Wang
mesh_terms: D020816:Amino Acid Motifs / Q000235:genetics*; D019943:Amino Acid Substitution; D000818:Animals; D002522:Chlorocebus aethiops; D012321:DNA-Directed RNA Polymerases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D017930:Genes, Reporter; D049452:Green Fluorescent Proteins / Q000096:biosynthesis / Q000235:genetics; D009154:Mutation; D045405:Nipah Virus / Q000235:genetics*; D014709:Vero Cells; D014764:Viral Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D014779:Virus Replication
chemical_list: D014764:Viral Proteins; C485184:enhanced green fluorescent protein; D049452:Green Fluorescent Proteins; C435063:L protein, Nipah virus; D012321:DNA-Directed RNA Polymerases