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...

Descripción completa

Detalles Bibliográficos
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
Descripción
Sumario: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.

Ejemplares similares