The I22V and L72S substitutions in West Nile virus prM protein promote enhanced prM/E heterodimerisation and nucleocapsid incorporation

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-immunopr...

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Autores principales: Setoh, Yin Xiang, Tan, Cindy Si En, Prow, Natalie A, Hobson-Peters, Jody, Young, Paul R, Khromykh, Alexander A, Hall, Roy A
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2015
Materias:
Short Report
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4424586/
https://www.ncbi.nlm.nih.gov/pubmed/25946997
http://dx.doi.org/10.1186/s12985-015-0303-7
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author Setoh, Yin Xiang
Tan, Cindy Si En
Prow, Natalie A
Hobson-Peters, Jody
Young, Paul R
Khromykh, Alexander A
Hall, Roy A
author_facet Setoh, Yin Xiang
Tan, Cindy Si En
Prow, Natalie A
Hobson-Peters, Jody
Young, Paul R
Khromykh, Alexander A
Hall, Roy A
author_sort Setoh, Yin Xiang
collection PubMed
description 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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spelling pubmed-44245862015-05-09 The I22V and L72S substitutions in West Nile virus prM protein promote enhanced prM/E heterodimerisation and nucleocapsid incorporation Setoh, Yin Xiang Tan, Cindy Si En Prow, Natalie A Hobson-Peters, Jody Young, Paul R Khromykh, Alexander A Hall, Roy A Virol J Short Report 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. BioMed Central 2015-05-07 /pmc/articles/PMC4424586/ /pubmed/25946997 http://dx.doi.org/10.1186/s12985-015-0303-7 Text en © Setoh et al.; licensee BioMed Central. 2015 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Short Report
Setoh, Yin Xiang
Tan, Cindy Si En
Prow, Natalie A
Hobson-Peters, Jody
Young, Paul R
Khromykh, Alexander A
Hall, Roy A
The I22V and L72S substitutions in West Nile virus prM protein promote enhanced prM/E heterodimerisation and nucleocapsid incorporation
title The I22V and L72S substitutions in West Nile virus prM protein promote enhanced prM/E heterodimerisation and nucleocapsid incorporation
title_full The I22V and L72S substitutions in West Nile virus prM protein promote enhanced prM/E heterodimerisation and nucleocapsid incorporation
title_fullStr The I22V and L72S substitutions in West Nile virus prM protein promote enhanced prM/E heterodimerisation and nucleocapsid incorporation
title_full_unstemmed The I22V and L72S substitutions in West Nile virus prM protein promote enhanced prM/E heterodimerisation and nucleocapsid incorporation
title_short The I22V and L72S substitutions in West Nile virus prM protein promote enhanced prM/E heterodimerisation and nucleocapsid incorporation
title_sort i22v and l72s substitutions in west nile virus prm protein promote enhanced prm/e heterodimerisation and nucleocapsid incorporation
topic Short Report
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4424586/
https://www.ncbi.nlm.nih.gov/pubmed/25946997
http://dx.doi.org/10.1186/s12985-015-0303-7
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