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        Expression Profiling of WSSV ORF 199 and Shrimp Ubiquitin Conjugating Enzyme in WSSV Infected Penaeus monodon

        Jeena, K.,Prasad, K. Pani,Pathan, Mujahid Khan,Babu, P. Gireesh Asian Australasian Association of Animal Productio 2012 Animal Bioscience Vol.25 No.8

        White spot syndrome virus (WSSV) is one of the major viral pathogens affecting shrimp aquaculture. Four proteins, WSSV199, WSSV 222, WSSV 249 and WSSV 403, from WSSV are predicted to encode a RING-H2 domain, which in presence of ubiquitin conjugating enzyme (E2) in shrimp 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, a time course expression profile analysis of WSSV Open Reading Frame (ORF) 199 and Penaeus monodon ubiquitin conjugating enzyme (PmUbc) was carried out at 0, 3, 6, 12, 24, 48 and 72 h post WSSV challenge by semi-quantitative RT-PCR as well as Real Time PCR. EF1${\alpha}$ was used as reference control to normalize the expression levels. A significant increase in PmUbc expression at 24 h post infection (h.p.i) was observed followed by a decline till 72 h.p.i. Expression of WSSV199 was observed at 24 h.p.i in WSSV infected P. monodon. Since the up-regulation of PmUbc was observed at 24 h.p.i where WSSV199 expression was detected, it can be speculated that these proteins might interact with host ubiquitination pathway for viral pathogenesis. However, further studies need to be carried out to unfold the molecular mechanism of interaction between host and virus to devise efficient control strategies for this chaos in the shrimp culture industry.

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        Cloning, expression, molecular modelling and docking analysis of steroidogenic acute regulatory protein (StAR) in Clarias batrachus

        Irfan Ahmad Bhat,Rupam Sharma,Mohd Ashraf Rather,Pravesh Kumar Rathor,P. Gireesh‑Babu,Mukunda Goswami,J. K. Sundaray 한국유전학회 2017 Genes & Genomics Vol.39 No.9

        The steroidogenic acute regulatory protein (StAR) plays a key role in transferring cholesterol across the inner mitochondrial membrane. In this study, the StAR gene was isolated from the gonads of Clarias batrachus. The gene has an open reading frame of 857 bp and encodes 285 amino acids with a predicted molecular weight of 32 kDa. The signalP analysis predicted that StAR would be a non-secreted protein that lacks a signal peptide. The subcellular localization demonstrated that the presence of the StAR protein was higher in mitochondria (41.8%), followed by the nuclear region (37.1%) and cytoplasm (11.1%). The StAR protein was found to interact highly with cyp11a1, followed by the cytochrome P450 family 11 proteins and the START5 domain. The homology modelling revealed that the protein has 4 helices and twisted U-shaped 10 beta sheets numbered from αA to αD and β1 to β10, respectively. Molecular modelling analysis showed that resveratrol and eurycomanone has high binding affinity with the StAR protein. The C. batrachus StAR transcript was found to be expressed exclusively in the gonads, kidney, and liver. These results overall lay a solid foundation for understanding the structure of StAR protein in fish. The identification of 3D structures and binding sites will help in designing a structure-based drug of StAR agonists for the treatment of impaired steroidogenesis.

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