Shrimp arginine kinase being a binding protein of WSSV envelope protein VP31

Cuiyan Ma; Qiang Gao; Yan Liang; Chen Li; Chao Liu; Jie Huang

doi:10.1007/s00343-016-5198-7

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Shrimp arginine kinase being a binding protein of WSSV envelope protein VP31

Updated：2023-05-16

- Shrimp arginine kinase being a binding protein of WSSV envelope protein VP31
- Journal of Oceanology and Limnology Vol. 34, Issue 6, Pages: 1287-1296(2016)
- Affiliations：
  
  1. Yellow Sea Fisheries Research Institute Chinese Academy of Fishery Sciences
  2. National Laboratory for Marine Science and Technology
- Author bio：
- Funds：
- DOI：10.1007/s00343-016-5198-7
  CLC：
- Online First：17 March 2016，
  
  Published：2016
- Accepted：
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Ma, C., Gao, Q., Liang, Y. et al. Shrimp arginine kinase being a binding protein of WSSV envelope protein VP31., Chin. J. Ocean. Limnol. 34, 1287–1296 (2016). https://doi.org/10.1007/s00343-016-5198-7
DOI：

Ma, C., Gao, Q., Liang, Y. et al. Shrimp arginine kinase being a binding protein of WSSV envelope protein VP31., Chin. J. Ocean. Limnol. 34, 1287–1296 (2016). https://doi.org/10.1007/s00343-016-5198-7 DOI：

摘要

Abstract

Viral entry into the host is the earliest stage of infection in the viral life cycle in which attachment proteins play a key role. VP31 (WSV340/WSSV396)

an envelope protein of white spot syndrome virus (WSSV)

contains an Arg-Gly-Asp (RGD) peptide domain known as a cellular attachment site. At present

the process of VP31 interacting with shrimp host cells has not been explored. Therefore

the VP31 gene was cloned into pET30a (+)

expressed in Escherichia coli strain BL21 and purified with immobilized metal ion affinity chromatography. Four gill cellular proteins of shrimp (Fenneropenaeus chinensis) were pulled down by an affinity column coupled with recombinant VP31 (rVP31)

and the amino acid sequences were identified with MALDI-TOF/TOF mass spectrometry. Hemocyanin

beta-actin

arginine kinase (AK)

and an unknown protein were suggested as the putative VP31 receptor proteins. SDS-PAGE showed that AK is the predominant binding protein of VP31. An i n vitro binding activity experiment indicated that recombinant AK’s (rAK) binding activity with rVP31 is comparable to that with the same amount of WSSV. These results suggested that AK

as a member of the phosphagen kinase family

plays a role in WSSV infection. This is the first evidence showing that AK is a binding protein of VP31. Further studies on this topic will elucidate WSSV infection mechanism in the future.

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references

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