3 years ago

Intrinsically Disordered HTLV-1 p30 protein: Experimental and Computational Evidence.

Priyanka Namdev, Denzelle Lee Lyngdoh, Hamid Yousf Dar, Shivendra K Chaurasiya, Rupesh Srivastava, Timir Tripathi, Rajaneesh Anupam
Human T lymphotropic virus type 1 (HTLV-1) causes adult T-cell leukemia and lymphoma (ATL) and other neuroinflammatory diseases. The pX region of HTLV-1 genome encodes an accessory protein p30 that is required for viral persistence and spread in the host. p30 regulates viral gene expression at the transcription level by competing with Tax for p300 binding and at post transcriptional level by nuclear retention of tax/rex mRNA. In addition, p30 modulates the host cellular environment by binding to various host proteins such as ATM, REGγ, PRMT5, etc. However, the low expression levels of p30 has been a major hurdle in studying its structure-function relationship in the context of HTLV-1 pathobiology, which is most likely due to its intrinsically disordered nature. In order to investigate the unstable nature of p30, flow cytometric analysis of p30-GFP fusion protein expressed in Escherichia coli (E. coli) was conducted and bioinformatics analysis of p30 was performed. The bacterial cells were GFP positive indicating that p30-GFP was in the soluble fraction. Induction, particularly at higher temperature reduced the expression of p30-GFP. Moreover, p30-GFP was detected exclusively in insoluble fraction upon cell lysis suggesting its unstable and disordered nature. The bioinformatic analysis of p30 protein sequence and amino acid content revealed that p30 has highly disordered regions from amino acids 75-155 and 197-241. Further, p30 has regions for macromolecular interactions that could stabilize it and these regions coincide with the unstable regions. Collectively, the study indicates that HTLV-1 p30 is an intrinsically disordered protein (IDP).

Publisher URL: http://doi.org/10.1089/AID.2018.0196

DOI: 10.1089/AID.2018.0196

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