Oncotarget

Research Papers:

Bovine herpesvirus 1 tegument protein UL21 plays critical roles in viral secondary envelopment and cell-to-cell spreading

Farzana Shahin, Sohail Raza, Kui Yang, Changmin Hu, Yingyu Chen, Huanchun Chen and Aizhen Guo _

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Oncotarget. 2017; 8:94462-94480. https://doi.org/10.18632/oncotarget.21776

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Abstract

Farzana Shahin1,2, Sohail Raza1,2,6, Kui Yang3, Changmin Hu2, Yingyu Chen2, Huanchun Chen1,2 and Aizhen Guo1,2,4,5

1The State Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, China

2College of Veterinary Medicine, Huazhong Agricultural University, Wuhan 430070, China

3Department of Pathobiological Sciences, School of Veterinary Medicine, Louisiana State University, Baton Rouge, Louisiana 70803, USA

4Key Laboratory of Development of Veterinary Diagnostic Products, Ministry of Agriculture, Wuhan 430070, China

5Hubei International Scientific and Technological Cooperation Base of Veterinary Epidemiology, Huazhong Agricultural University, Wuhan 430070, China

6Department of Microbiology, University of Veterinary and Animal Sciences, Lahore 54000, Pakistan

Correspondence to:

Aizhen Guo, email: aizhen@mail.hzau.edu.cn

Keywords: BoHV-1, interacting proteins, secondary envelopment, tegument, UL21

Received: July 13, 2017     Accepted: September 21, 2017     Published: October 10, 2017

ABSTRACT

Bovine herpesvirus 1 (BoHV-1) UL21 is a tegument protein thought to be indispensable for efficient viral growth but its precise function in BoHV-1 is currently unknown. To determine the function of UL21 in BoHV-1 replication, we constructed a mutant virus bearing a UL21 deletion (vBoHV-1-ΔUL21) and its revertant virus, vBoHV-1-ΔUL21R, in which the UL21 gene was restored using a bacterial artificial chromosome system. The replication of vBoHV-1-ΔUL21 was 1,000-fold lower and its plaque size was 85% smaller than those of the wild-type virus (BoHV-1). An ultrastructural analysis showed that deletion of UL21 led to an un-enveloped capsid accumulation in the cytoplasm, whereas nucleocapsid egress was not impaired, suggesting that UL21 is critical for secondary envelopment in BoHV-1. Co-immunoprecipitation assays revealed that HA-tagged UL21 pulled down UL16, suggesting that these two proteins form a complex, and this was further confirmed by a co-immunofluorescence assay. Taken together, these data provide evidence that UL21 plays critical roles in BoHV-1 secondary envelopment, and UL16 is likely to be involved in these activities.


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