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Cellular protein p32/gC1qR recruits PKC to Viral Protein ICP34.5 and Facilitates HSV Nuclear Egress
Author(s) -
Zhang Cuizhu,
Wu Songfang,
Wang Yu,
Zhang Liming,
Pan Shuang,
Liu Yaohui,
Yang Mengmeng,
Chen Da,
Wang Jiyan,
He Bin,
Cao Youjia
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.760.20
Subject(s) - herpes simplex virus , viral replication , nuclear protein , microbiology and biotechnology , nuclear lamina , biology , cytoplasm , virology , budding , virus , nuclear transport , gene , cell nucleus , genetics , transcription factor
The nuclear envelop is considered anatural barrier of virus budding and efficient replication. Several lines of evidence suggest that the disruption of the integrity of nuclear lamina correlate with the nucleocapsid budding of herpesviruses. Mammalian cellular protein p32 is identified as a new target for Herpes simplex virus 1 (HSV‐1)virulent protein, ICP34.5. We found that the efficient nuclear egress of HSV‐1 particles was impaired in the absence of cellular p32 protein. Lacking ICP34.5 encoding gene in HSV‐1 or reduced expression of host p32 severely affects viral replication. Here we report that the interaction betweenp32 and ICP34.5 of HSV‐1 facilitates nucleocapsid release to the cytoplasm. P32binds to the NH2‐terminus of ICP34.5 and recruits PKC to the nuclear lamina, where LaminA/C is phosphorylated and nuclear integrity disturbed. Unlike wildtype virus, an HSV mutant devoid of ICP34.5 or its amino‐terminus is crippled for viral growth and release. This is attributable to a defect in virus nuclear egress. In HSV infected cells, p32 is recruited to the nuclear membrane and triggers PKC activation whereas in cells infected by HSV with ICP34.5 mutants fail to exert any effect. These results suggest that disintegration of the nuclear lamina mediated by the association of p32 and ICP34.5 promotes HSV replication via PKC. Support or Funding Information This work was supported by the National Natural Science Foundation of China (31370862; 81672010 to YC)