The capsid protein encoded by U(L)17 of herpes simplex virus 1 interacts with tegument protein VP13/14.
The capsid protein encoded by U(L)17 of herpes simplex virus 1 interacts with tegument protein VP13/14.
复制标题
单纯疱疹病毒 1 型 U(L)17 编码的衣壳蛋白与被膜蛋白 VP13/14 相互作用。
DOI:
10.1128/jvi.00277-10
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发表时间:
2010
影响因子:
5.4
通讯作者:
Baines,JoelD
中科院分区:
文献类型:
--
作者:
Scholtes,LuellaD;Yang,Kui;Li,LucyX;Baines,JoelD
The UL17 protein (pUL17) of herpes simplex virus 1 (HSV-1) likely associates with the surfaces of DNA-containing capsids in a heterodimer with pUL25. pUL17 is also associated with viral light particles that lack capsid proteins, suggesting its presence in the tegument of the HSV-1 virion. To help determine how pUL17 becomes incorporated into virions and its functions therein, we identified pUL17-interacting proteins by immunoprecipitation with pUL17-specific IgY at 16 h postinfection, followed by mass spectrometry. Coimmunoprecipitated proteins included cellular histone proteins H2A, H3, and H4; the intermediate filament protein vimentin; the major HSV-1 capsid protein VP5; and the HSV tegument proteins VP11/12 (pUL46) and VP13/14 (pUL47). The pUL17-VP13/14 interaction was confirmed by coimmunoprecipitation in the presence and absence of intact capsids and by affinity copurification of pUL17 and VP13/14 from lysates of cells infected with a recombinant virus encoding His-tagged pUL17. pUL17 and VP13/14-HA colocalized in the nuclear replication compartment, in the cytoplasm, and at the plasma membrane between 9 and 18 h postinfection. One possible explanation of these data is that pUL17 links the external face of the capsid to VP13/14 and associated tegument components.