2012 OSU Molecular Life Sciences
Interdisciplinary Graduate Programs Symposium
Poster abstracts
Abstract:
Background: Human T lymphotrophic virus type-1 (HTLV-1) and type 2 (HLTV-2) are related human retroviruses. HTLV-1 is the causative agent of aggressive T-cell leukemia known as adult T-cell leukemia (ATL), HTLV-1 associated myelopathy/tropical spastic paraparesis (HAM/TSP), and other inflammatory diseases. HTLV-2 infection has not been clearly associated with any disease condition. Although both viruses can transform T cells in vitro, the HTLV-1 provirus is mainly detected in CD4+ T cells whereas HTLV-2 is mainly detected in CD8+ T cells in infected individuals. HTLV-1 and HTLV-2 encode accessory proteins p30 and p28, respectively, which are required for viral persistence in vivo. The goal of this study was to identify host proteins interacting with p30 and p28.
Results: Affinity-tag purification coupled with mass spectrometric (MS) analysisrevealed a series of host proteins binding to p30 and p28. To validate the proteomic results four interacting proteins were selected for further analysis with immnoblot assays. Of these, two cellular proteins REGγ and NEAF-interacting protein 30 (NIP30) selectively interacted with p30 and not with p28. Conversely, heterogeneous nuclear ribonucleoprotein H1 (hnRNP H1) bound to p28 and not to p30. Another cellular protein arginine methylatransferase 5 (PRMT5) interacted with both p30 and p28.
Conclusion: The comparisons of p30 and p28 host protein interaction profiles shows major differences with some degree of overlap. These findings suggest that the difference in the host protein interaction profiles of p30 and p28 would in part be responsible for different HTLV-1 and HTLV-2 pathobiology.
Keywords: HTLV-1 p30, HTLV-2 p28, Host proteins interaction, hnRNP H1, PRMT5, Nip30