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. and Hall, Roy A. (2015) The I22V and L72S substitutions in West Nile virus prM protein promote enhanced prM/E heterodimerisation and nucleocapsid incorporation. Virology Journal, 12 1: 72.1-72.5. doi:10.1186/s12985-015-0303-7


Author Setoh, Yin Xiang
Tan, Cindy Si En
Prow, Natalie A.
Hobson-Peters, Jody
Young, Paul R.
Khromykh, Alexander A.
Hall, Roy A.
Title The I22V and L72S substitutions in West Nile virus prM protein promote enhanced prM/E heterodimerisation and nucleocapsid incorporation
Journal name Virology Journal   Check publisher's open access policy
ISSN 1743-422X
Publication date 2015-05-07
Sub-type Article (original research)
DOI 10.1186/s12985-015-0303-7
Open Access Status DOI
Volume 12
Issue 1
Start page 72.1
End page 72.5
Total pages 5
Place of publication London, United Kingdom
Publisher BioMed Central
Collection year 2016
Language eng
Formatted abstract
Background: Amino acid substitutions I22V and L72S in the prM protein of West Nile virus Kunjin strain (WNVKUN) 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.
Keyword Flavivirus
Heterodimerisation
prM
West Nile virus
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2016 Collection
School of Chemistry and Molecular Biosciences
 
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Created: Fri, 19 Jun 2015, 13:05:52 EST by Anthony Yeates on behalf of School of Chemistry & Molecular Biosciences