Abstract
The Bas-Congo virus (BASV) is the first rhabdovirus associated with a human outbreak of acute hemorrhagic fever. The single-stranded, negative-sense RNA genome of BASV contains the five core genes present in all rhabdoviral genomes plus an additional three genes, annotated U1, U2, and U3, with weak (<21%) sequence similarity only to a handful of genes observed in a few other rhabdoviral genomes. The function of the rhabdoviral U proteins is unknown, but, they are hypothesized to play a role in viral infection or replication. To better understand this unique family of proteins, a construct containing residues 27–203 of the 216-residue U1 protein (BASV-U1*) was prepared. By collecting data in 0.5 M urea it was possible to eliminate transient association enough to enable the assignment of most of the observable 1HN, 1Hα, 15N, 13Cα, 13Cβ, and 13C´ chemical shifts for BASV-U1* that will provide a foundation to study its solution properties. The analyses of these chemical shifts along with 15N-edited NOESY data enabled the identification of the elements of secondary structure present in BASV-U1*.
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Borio L, Inglesby T, Peters CJ, Schmaljohn AL, Hughes JM, Jahrling PB, Ksiazek T, Johnson KM, Meyerhoff A, O'Toole T, Ascher MS, Bertlett J, Breman JG, Eitzen EM, Hamburg M, Hauer J, Henderson DA, Johnson RT, Kwik G, Layton M, Lillibridge S, Nabel GJ, Osterholm MT, Perl TM, Russell P, Tonat (2002) Hemorrhagic fever viruses as biological weapons: medical and public health management. JAMA 297:2391–2405
Buchko GW, Edwards TE, Hewitt SN, Phan IQH, Van Voorhis WC, Miller SI, Myler PJ (2015) Backbone chemical shift assignments for the sensor domain of the Burkholderia pseudomallei histidine kinase RisS: “missing” resonances at the dimer interface. J Biomol NMR Assign 9:381–385
Buchko GW, Perkins A, Parsonage D, Poole LB, Karplus PA (2016) Backbone chemical shift assignment for Xanthomonas campestris peroxiredoxin Q in the reduced and oxidized states: a dramatic change in backbone dynamics. J Biomol NMR Assign 10:57–61
Chae YK, Im H, Zhao Q, Doelling JH, Vierstra RD, Markley JL (2004) Prevention of aggregation after refolding by balanced stabilization-destabilization: production of Arabidopsis thaliana protein APG8a (At4g21980) for NMR structure determination. Prot Express Purif 34:280–283
Drozdetskiy A, Cole C, Procter J, Barton GJ (2015) JPred4: a protein secondary structure prediction server. Nucl Acids Res 43:W389–W394
Gardner KH, Rosen MK, Kay LE (1997) Global folds of highly deuterated, methyl protonated proteins by multidimensional NMR. Biochemistry 36:1389–1401
Grard G, Fair JN, Lee D, Slikas E, Steffen I, Muyembe J-J, Sittler T, Veeraraghavan N, Ruby JG, Wang C, Makuwa M, Mulembakani P, Tesh RB, Mazet J, Rimoin AW, Taylor T, Schneider BS, Simmons G, Delwart E, Wolfe ND, Chiu CY, Leroy EM (2012) A novel rhabdovirus associated with acute hemorrhagic fever in Central Africa. PLoS Pathog 8:e1002924
Gubala A, Davis S, Weir R, Melvelle L, Cowled C, Boyle D (2011) Tibrogargan and coastal plains rhabdoviruses: genomic characterization, evolution of novel genes and seroprevalence in Australian livestock. J Gen Virol 92:2160–2170
Hafsa NE, Arndt D, Wishart DS (2015) CSI 3.0: a web server for identifying secondary and super-secondary structure in proteins using NMR chemical shifts. Nucleic Acids Res 43:W370–W377
Kuzmin IV, Novella IS, Dietzgen RG, Padhi A, Rupprecht CE (2009) The rhabdoviruses: biodiversity, phylogenetics, and evolution. Infect Genet Evol 9:541–553
Müller CW, Schlauderer GJ, Reinstein J, Schulz GE (1992) Adenylate kinase motions during catalysis: an energetic counterweight balancing substrate binding. Structure 4:147–156
Paessler S, Walker DH (2013) Pathogenesis of the viral hemorrhagic fevers. Annu Rev Pathol Mech Dis 8:411–440
Stremlau MH, Andersen KG, Folarin OA, Grove JN, Odia I, Ehiane PE, Omoniwa O, Omoregie O, Jiang P-P, Yozwiak NL, Matranga CB, Yang X, Gire SK, Winnicki S, Tariyal R, Schaffner SF, Okokhere PO, Okogbenin S, Akpede GO, Asogun DA, Agbonlahor DE, Walker PJ, Tesh RB, Levin JZ, Garry RF, Sabeti PC, Happi CT (2015) Discovery of novel rhabdoviruses in the blood of healthy individuals from West Africa. PLoS Negl Trop Dis 9:e0003631
Yee A, Chang X, Pineda-Lucena A, Wu B, Semesi A, Le B, Ramelot T, Lee GM, Bhattacharyya S, Gutierrez P, Denisov A, Lee C-H, Cort JR, Kozlov G, Liao J, Finak G, Chen L, Wishart D, Lee W, McIntosh LP, Gehring K, Kennedy MA, Edwards AM, Arrowsmith CH (2002) An NMR approach to structural proteomics. Proc Natl Acad Sci USA 99:1825–1930
Acknowledgements
This research was supported by the National Institute of Allergy and Infectious Diseases under Federal Contract No. HHSN2722001200025C. The SSGCID internal ID for the BASV-U1* protein construct is RhbaA.18619.a.D16, a community request from Dr. Charles Y. Chiu at the University of California in San Francisco. A large part of this research was performed at the W. R. Wiley Environmental Molecular Sciences Laboratory (EMSL), a national scientific user facility located at Pacific Northwest National Laboratory (PNNL) and sponsored by U.S. Department of Energy’s Office of Biological and Environmental Research (BER) program. Battelle operates PNNL for the U.S. Department of Energy.
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Buchko, G.W., Clifton, M.C., Wallace, E.G. et al. Backbone chemical shift assignments and secondary structure analysis of the U1 protein from the Bas-Congo virus. Biomol NMR Assign 11, 51–56 (2017). https://doi.org/10.1007/s12104-016-9719-2
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DOI: https://doi.org/10.1007/s12104-016-9719-2