Expression Profile of Penaeus monodon Ubiquitin Conjugating Enzyme (PmUbc) at Protein Level in White spot syndrome virus Challenged Shrimp

Abstract

White spot syndrome virus (WSSV) is one of the major pathogens in shrimp aquaculture. Four proteins of WSSV are predicted to encode a RING H2 domain, which in presence of ubiquitin conjugating enzyme (E2) in shrimps can function as viral E3 ligase and modulate the host ubiquitin proteasome pathway. Modulation of host ubiquitin proteasome pathway by viral proteins is implicated in viral pathogenesis. In the present study, expression profile of Penaeus monodon Ubiquitin conjugating enzyme (PmUbc) was studied at protein level in WSSV challenged shrimp. A time point analysis of the expression of PmUbc was carried out at 0, 3, 6, 12, 24, 48 and 72 h post WSSV challenge in P. monodon. Recombinant PmUbc (rPmUbc) was produced in prokaryotic expression vector, BL21 (DE3) pLys S. The PmUbc expression pattern was studied by ELISA with rPmUbc antibodies raised in rabbit. A significant increase in PmUbc expression at 24 h post infection (hpi) was observed followed by a decline till 72 hpi. Since the up-regulation and a tremendous decline of PmUbc protein expression was observed at 24 and in 72 hpi respectively in ELISA, it can be speculated that these proteins might interact with host ubiquitination pathway for viral pathogenesis. Many findings have shown that viral infection can up-regulate expression of ubiquitin and that the ubiquitin system plays a key role in the course of viral infection. The present study reveals the expression patterns of PmUbc at protein level in WSSV infected P. monodon. However, further studies are to be carried out to unfold the molecular mechanism of interaction between host and virus to devise efficient control strategies for this major culprit in shrimp culture industry.

Differential expression of proteins in the gills of Litopenaeus vannamei infected with white spot syndrome virus

“…Their study also revealed a weak expression of PvUbc in uninfected shrimp, suggesting that PvUbc expression is induced in WSSV infection till 48 h.a.i. Keezhedath et al (2013), the ubiquitin increased expression in P. monodon (PmUbc) post WSSV infection. In our study, the groups 24 and 72 h.a.i., ubiquitin protein had greater expression, agreeing with the findings of the authors cited above.…”

A transcriptome study on Macrobrachium nipponense hepatopancreas experimentally challenged with white spot syndrome virus (WSSV)

“…This pathway also participated in viral infection and assists activities required of different aspect of virus life cycle, such as entry, replication and shedding [ 94 ]. Recently, various reports have been conducted showing the hijack of UPP pathway to regulate cellular intrinsic antiviral activities and innate immunity induced by WSSV [ 95 , 96 ]. E3 ubiquitin-protein ligase HUWE1 with the highest up changes after WSSV chanllenge was found in M .…”

Ubiquitination as an Important Host-Immune Response Strategy in Penaeid Shrimp: Inferences From Other Species

“…The synthesis presented in this paper provides a snapshot of ubiquitination as a host-pathogen immune response strategy in shrimp. Most current studies have shown that microbial infection of shrimp could induce ubiquitination through ubiquitin-conjugating enzymes, ubiquitin ligases, or ubiquitinated substrates ( 64 , 85 , 104 ). On the one hand, the ubiquitin system in shrimp could be exploited as a mechanism to resist pathogen invasion or annexed by microbial pathogens for replication and survival.…”

“…Some viral proteins act as E3 ubiquitin ligases to promote viral infection and survival using the host ubiquitin system. The RING proteins of WSSV, including WSSV199, WSSV222, WSSV249, and WSSV403, could serve as E3 ligases to coopt the ubiquitin-proteasome pathway of shrimp for viral replication ( 74 , 76 , 104 ). Furthermore, WSSV249 acts as an E3 ligase through interaction of ubiquitin-conjugating enzyme E2 for viral pathogenesis in P. vannamei ( 105 ).…”