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A structural DNA binding protein of African swine fever virus with similarity to bacterial histone-like proteins

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Summary

Here we describe an African swine fever virus (ASFV) protein encoded by the open reading frame 5-AR that shares structural and functional similarities with the family of bacterial histone-like proteins which include histone-like DNA binding proteins, integration host factor, andBacillus phage SPO1 transcription factor, TF1. The ASFV 5-AR gene was cloned by PCR and expressed inE. coli. Monospecific antiserum prepared to the 5-AR bacterial expression product specifically immunoprecipitated a protein of approximately 11.6 kDa from ASFV infected swine macrophages at late times post-infection. Additionally, the 5-AR expression product was strongly recognized by ASFV convalescent pig serum, indicating its antigenicity during natural infection. Cloned p11.6 bound both double and single stranded DNA-cellulose columns. Consistent with a DNA binding function, immunoelectronmicroscopy localized p11.6 to the virion nucleoid. To our knowledge, p11.6 is the first bacterial histone-like DNA-binding protein found in an animal virus or eukaryotic cell system.

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Authors and Affiliations

  1. ARS, USDA, Plum Island Animal Disease Center, Greenport, New York, USA

    M. V. Borca, P. M. Irusta, G. F. Kutish, C. Carrillo, C. L. Afonso, T. Burrage, J. G. Neilan & D. L. Rock

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  1. M. V. Borca
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  2. P. M. Irusta
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  3. G. F. Kutish
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  4. C. Carrillo
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  5. C. L. Afonso
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  6. T. Burrage
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  7. J. G. Neilan
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  8. D. L. Rock
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Borca, M.V., Irusta, P.M., Kutish, G.F. et al. A structural DNA binding protein of African swine fever virus with similarity to bacterial histone-like proteins. Archives of Virology 141, 301–313 (1996). https://doi.org/10.1007/BF01718401

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  • DOI: https://doi.org/10.1007/BF01718401

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