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西尼罗河病毒prM蛋白中的I22V和L72S替换促进了prM/E异源二聚化增强及核衣壳掺入。

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

作者信息

Setoh Yin Xiang, Tan Cindy Si En, Prow Natalie A, Hobson-Peters Jody, Young Paul R, Khromykh Alexander A, Hall Roy A

机构信息

Australian Infectious Diseases Research Centre, School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, QLD, 4072, Australia.

Present Address: Sir Albert Sakzewski Virus Research Centre, Clinical Medical Virology Centre, Herston, QLD, Australia.

出版信息

Virol J. 2015 May 7;12:72. doi: 10.1186/s12985-015-0303-7.

DOI:10.1186/s12985-015-0303-7
PMID:25946997
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4424586/
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.

摘要

背景

先前研究表明，西尼罗河病毒库京株（WNVKUN）的prM蛋白中的氨基酸替换I22V和L72S可增强病毒分泌和毒力，但未确定其发生机制。

研究结果

通过脉冲追踪实验，随后用抗E抗体进行共免疫沉淀，我们证明I22V和L72S替换增强了E糖基化和E非糖基化病毒的prM/E异源二聚化。此外，对分泌颗粒的分析表明，I22V和L72S替换也增强了核衣壳的掺入。

结论

我们已从机制上证明，在存在I22V和L72S替换的情况下，病毒颗粒分泌的改善是由更有效的prM/E异源二聚化所致。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1a24/4424586/82944101b2d4/12985_2015_303_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1a24/4424586/c8d4e5ac494f/12985_2015_303_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1a24/4424586/c37daa00489b/12985_2015_303_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1a24/4424586/c0a9a69cdc6d/12985_2015_303_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1a24/4424586/82944101b2d4/12985_2015_303_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1a24/4424586/c8d4e5ac494f/12985_2015_303_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1a24/4424586/c37daa00489b/12985_2015_303_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1a24/4424586/c0a9a69cdc6d/12985_2015_303_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1a24/4424586/82944101b2d4/12985_2015_303_Fig4_HTML.jpg

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2
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J Gen Virol. 2012 Sep;93(Pt 9):1965-1975. doi: 10.1099/vir.0.044453-0. Epub 2012 Jul 4.
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Class II ADP-ribosylation factors are required for efficient secretion of dengue viruses.
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J Biol Chem. 2012 Jan 2;287(1):767-777. doi: 10.1074/jbc.M111.270579. Epub 2011 Nov 21.
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