Research Papers: Immunology:

A bovine herpesvirus 1 pUL51 deletion mutant shows impaired viral growth in vitro and reduced virulence in rabbits

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

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Oncotarget. 2016; 7:12235-12253. https://doi.org/10.18632/oncotarget.7771

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Sohail Raza1,2, Mingliang Deng1,2, Farzana Shahin1,2, Kui Yang3, Changmin Hu1,2, Yingyu Chen1,4, Huanchun Chen1,2 and Aizhen Guo1,2,5,6

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

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

3 Department of Pathobiological Sciences, School of Veterinary Medicine, Louisiana State University, Baton Rouge, Louisiana, United States of America

4 College of Animal Science and Technology, Huazhong Agricultural University, Wuhan, China

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

6 International Joint Research and Training Centre for Veterinary Epidemiology, Hubei Province, Wuhan, China

Correspondence to:

Aizhen Guo, email:

Keywords: bovine herpesvirus 1, bacterial artificial chromosome, morphogenesis, pUL51, tegument protein, Immunology and Microbiology Section, Immune response, Immunity

Received: November 19, 2015 Accepted: February 20, 2016 Published: February 26, 2016


Bovine herpesvirus 1 (BoHV-1) UL51 protein (pUL51) is a tegument protein of BoHV-1 whose function is currently unknown. Here, we aimed to illustrate the specific role of pUL51 in virion morphogenesis and its importance in BoHV-1 virulence. To do so, we constructed a BoHV-1 bacterial artificial chromosome (BAC). We used recombinant BAC and transgenic techniques to delete a major part of the UL51 open reading frame. Deletion of pUL51 resulted in severe viral growth defects, as evidenced by lower single and multi-step growth kinetics, reduced plaque size, and the accumulation of non-enveloped capsids in the cytoplasm of infected cells. Using tagged BoHV-1 recombinant viruses, it was determined that the pUL51 protein completely co-localized with the cis-Golgi marker protein GM-130. Taken altogether, pUL51 was demonstrated to play a critical role in BoHV-1 growth and it is involved in viral maturation and egress. Moreover, an in vivo analysis showed that the pUL51 mutant exhibited reduced virulence in rabbits, with no clinical signs, no nasal shedding of the virus, and no detectable serum neutralizing antibodies. Therefore, we conclude that the BoHV-1 pUL51 is indispensable for efficient viral growth in vitro and is essential for virulence in vivo.

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