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Fish Shellfish Immunol. 2018 Aug;79:130-139. doi: 10.1016/j.fsi.2018.05.003. Epub 2018 May 5.

Identification of Litopenaeus vannamei BiP as a novel cellular attachment protein for white spot syndrome virus by using a biotinylation based affinity chromatography method.

Author information

1
Tianjin Key Laboratory of Animal and Plant Resistance, Tianjin, 300387, PR China; College of Life Sciences, Tianjin Normal University, 393 West Binshui Road, Xiqing District, Tianjin, 300387, PR China.
2
College of Life Sciences, Tianjin Normal University, 393 West Binshui Road, Xiqing District, Tianjin, 300387, PR China.
3
Tianjin Center for Control and Prevention of Aquatic Animal Infectious Disease, 442 South Jiefang Road, Hexi District, Tianjin 300221, China.
4
Tianjin Key Laboratory of Animal and Plant Resistance, Tianjin, 300387, PR China; College of Life Sciences, Tianjin Normal University, 393 West Binshui Road, Xiqing District, Tianjin, 300387, PR China. Electronic address: skysjs@mail.tjnu.edu.cn.

Abstract

White spot syndrome virus (WSSV) is a dangerous threat to shrimp farming that also attacks a wide range of crustaceans. Knowledge of the surface protein-protein interactions between the pathogen and host is very crucial to unraveling the molecular pathogenesis mechanisms of WSSV. In this study, LvBiP (Litopenaeus vannamei immunoglobulin heavy-chain-binding protein) was identified as a novel WSSV binding protein of L. vannamei by a biotinylation based affinity chromatography method. By using pull-down and ELISA assays, the binding of recombinant LvBiP to WSSV was proved to be specific and ATP- dependent. The interaction was also confirmed by the result of co-immunoprecipitation assay. Immunofluorescence studies revealed the co-localization of LvBiP with WSSV on the cell surface of shrimp haemocytes. Additionally, LvBiP is likely to play an important role in WSSV infection. Treatment of gill cellular membrane proteins (CMPs) with purified rLvBiP and antibody that specifically recognizes LvBiP, led to a significant reduction in the binding of WSSV to gill CMPs. In the in vivo neutralization assay, rLvBiP and anti-LvBiP polyclonal antibody partially blocked the infection of WSSV. Taken together, the results indicate that LvBiP, a molecular chaperon of the HSP70 family, is a novel host factor involved at the step of attachment of the WSSV to the host cells and a potential candidate of therapeutic target.

KEYWORDS:

Biotinylation; Litopenaeus vannamei; Protein-protein interactions; Viral adhesion; White spot syndrome virus

PMID:
29738871
DOI:
10.1016/j.fsi.2018.05.003
[Indexed for MEDLINE]

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