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Title: Identification of conserved motifs in the Westnile virus envelope essential for particle secretion
Authors: Garg, H
Lee, R.T.C
Tek, N.O
Maurer-Stroh, S 
Joshi, A
Keywords: protein
small interfering RNA
virus envelope protein
virus envelope protein
disulfide bond
molecular model
protein analysis
protein structure
site directed mutagenesis
virus assembly
virus envelope
West Nile flavivirus
cell line
chemical structure
nucleotide sequence
protein conformation
protein motif
virus release
West Nile flavivirus
West Nile virus
Amino Acid Motifs
Cell Line
Conserved Sequence
DNA Mutational Analysis
Models, Molecular
Protein Conformation
Viral Envelope Proteins
Virus Release
West Nile virus
Issue Date: 2013
Citation: Garg, H, Lee, R.T.C, Tek, N.O, Maurer-Stroh, S, Joshi, A (2013). Identification of conserved motifs in the Westnile virus envelope essential for particle secretion. BMC Microbiology 13 (1) : 197. ScholarBank@NUS Repository.
Rights: Attribution 4.0 International
Abstract: Background: Enveloped viruses utilize cellular membranes to bud from infected cells. The process of virion assembly and budding is often facilitated by the presence of certain conserved motifs within viral proteins in conjunction with cellular factors. We hence examined the West Nile Virus (WNV) Envelope protein for the presence of any such motifs and their functional characterization. Results: We identified conserved 461PXAP 464 and 349YCYL352 motifs in the WNV envelope glycoprotein bearing resemblance to retroviral late domains. Disruptive mutations of PXAP to LAAL and of the highly conserved Cys350 in the YCYL motif, led to a severe reduction in WNV particle production. Similar motifs in case of retroviruses are known to interact with components of host sorting machinery like PXAP with Tsg101 and YXXL with Alix. However, in the case of WNV, siRNA mediated depletion of Alix or Tsg101 did not have an effect on WNV release. Molecular modeling suggested that while the 461PXAP 464 motif is surface accessible and could potentially interact with cellular proteins required for WNV assembly, the 349YCYL 352 motif was found to be internal with Cys350 important for protein folding via disulphide bonding. Conclusions: The conserved 461PXAP464 and 349YCYL352 motifs in the WNV envelope are indispensable for WNV particle production. Although these motifs bear sequence similarity to retroviral late domains and are essential for WNV assembly, they are functionally distinct suggesting that they are not the typical late domain like motifs of retroviruses and may play a role other than Alix/Tsg101 utilization/dependence. © 2013 Garg et al.; licensee BioMed Central Ltd.
Source Title: BMC Microbiology
ISSN: 14712180
DOI: 10.1186/1471-2180-13-197
Rights: Attribution 4.0 International
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