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Backbone ¹⁵N relaxation analysis of the N-terminal domain of the HTLV-I capsid protein and comparison with the capsid protein of HIV-1

¹ Laboratory of Biophysical Chemistry, National Heart, Lung, and Blood Institute, NIH, Bethesda, Maryland 20892, USA
² Department of Molecular Genetics and Microbiology, State University of New York at Stony Brook, Stony Brook, New York 11794-5222, USA
³ Chemical Physics Program, University of Maryland, College Park, Maryland 20742-2431, USA

Reprint requests to: Nico Tjandra, Laboratory of Biophysical Chemistry, Bldg. 50, Room 3503, NHLBI, NIH, Bethesda, MD 20892, USA; e-mail: nico{at}helix.nih.gov; fax: (301) 402-3405; or Carol Carter, Department of Molecular Genetics and Microbiology, Life Sciences Bldg., SUNY at Stony Brook, Stony Brook, NY 11794-5222, USA; e-mail: ccarter{at}ms.cc.sunysb.edu; fax: (631) 632-9797.

Human T-cell leukemia virus type 1 (HTLV-I) is an oncogenic retrovirus that exhibits specific tropism for human T-cells. The capsid (CA) proteins of retroviruses share highly conserved secondary and tertiary structures. However, they can form quaternary structures (assembled cores) that are conical (e.g., the lentivirus subgroup, including HIV) or spherical (e.g., the oncovirus subgroup, including HTLV). The intrinsic features that drive these differences are not understood. So far, only structural studies have been used as a basis for comparison. Dynamics may play a role in particle formation. High-resolution nuclear magnetic resonance (NMR) ¹⁵N relaxation data (T₁, T₁, and NOE) have been used to characterize the backbone dynamics of the N-terminal domain (NTD) of the oncovirus HTLV-I and to compare with the CA NTD of HIV-1. Large variations in the ¹⁵N heteronuclear NOEs and transversal relaxation rates for individual residues are consistent with the bundle RMSD of the previously calculated NMR structures. The ß-hairpin and CyP-A loop exhibit different mobility in HTLV-I and HIV-1. The overall hydrodynamic property of the HTLV-I capsid NTD is quite distinct from the HIV-1.

Keywords: HTLV-I; capsid protein; retrovirus; NMR spectroscopy; relaxation; mutant; CyP-A

Abbreviations: HTLV-I, human T-cell leukemia virus type-I • HIV-1, human immunodeficiency virus type-I • CA, capsid • NTD, N-terminal domain • CyP-A, cyclophilin-A • NMR, nuclear magnetic resonance • NOE, nuclear Overhauser effect • RSV, Rous sarcoma virus • MLV, murine leukemia virus • T₁, spin-lattice relaxation time • T₁, spin-spin relaxation time • CPMG, Carr-Purcell-Meiboom-Gill • SD, standard deviation • psec, picosecond • _c, overall correlation time • S², order parameter

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