The capsid protein encoded by U(L)17 of herpes simplex virus 1 interacts with tegument protein VP13/14.

Abstract:

:The U(L)17 protein (pU(L)17) of herpes simplex virus 1 (HSV-1) likely associates with the surfaces of DNA-containing capsids in a heterodimer with pU(L)25. pU(L)17 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 pU(L)17 becomes incorporated into virions and its functions therein, we identified pU(L)17-interacting proteins by immunoprecipitation with pU(L)17-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 (pU(L)46) and VP13/14 (pU(L)47). The pU(L)17-VP13/14 interaction was confirmed by coimmunoprecipitation in the presence and absence of intact capsids and by affinity copurification of pU(L)17 and VP13/14 from lysates of cells infected with a recombinant virus encoding His-tagged pU(L)17. pU(L)17 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 pU(L)17 links the external face of the capsid to VP13/14 and associated tegument components.

journal_name

J Virol

journal_title

Journal of virology

authors

Scholtes LD,Yang K,Li LX,Baines JD

doi

10.1128/JVI.00277-10

subject

Has Abstract

pub_date

2010-08-01 00:00:00

pages

7642-50

issue

15

eissn

0022-538X

issn

1098-5514

pii

JVI.00277-10

journal_volume

84

pub_type

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