The I22V and L72S substitutions in West Nile virus prM protein promote enhanced prM/E heterodimerisation and nucleocapsid incorporation
Date
2015
Authors
Setoh, Y.X.
Tan, C.S.E.
Prow, N.A.
Hobson Peters, J.
Young, P.R.
Khromykh, A.A.
Hall, R.A.
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Journal article
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Virology Journal, 2015; 12(1, article number 72):1-5
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Abstract
Background: Amino acid substitutions I22V and L72S in the prM protein of West Nile virus Kunjin strain (WNV KUN ) were previously shown to enhance virus secretion and virulence, but a mechanism by which this occurred was not determined. Findings: Using pulse-chase experiments followed by co-immunoprecipitation with anti-E antibody, we demonstrated that the I22V and L72S substitutions enhanced prM/E heterodimerization for both the E-glycosylated and E-unglycosylated virus. Furthermore, analysis of secreted particles revealed that I22V and L72S substitutions also enhanced nucleocapsid incorporation. Conclusions: We have demonstrated mechanistically that improved secretion of virus particles in the presence of I22V and L72S substitutions was contributed by more efficient prM/E heterodimerization.
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Copyright 2015 The Authors. This is an Open Access article distributed under the terms of the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver applies to the data made available in this article,unless otherwise stated (http://creativecommons.org/licenses/by/4.0)