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A non-canonical Lon proteinase lacking the ATPase domain employs the Ser-Lys catalytic dyad to exercise broad control over the life cycle of a double-stranded RNA virus

  1. Author:
    Birghan, C.
    Mundt, E.
    Gorbalenya, A. E.

  2. Author Address

    Gorbalenya AE NCI, Frederick Canc Res & Dev Ctr, Adv Biomed Comp Ctr, SAIC Frederick, MD 21702 USA NCI, Frederick Canc Res & Dev Ctr, Adv Biomed Comp Ctr, SAIC Frederick, MD 21702 USA Fed Res Ctr Virus Dis Anim, Inst Mol Biol, Friedrich Loeffler Inst D-174988 Insel Riems Germany
    1. Year: 2000
  2. Journal: Embo Journal
    1. 19
    2. 1
    3. Pages: 114-123
  4. Type of Article: Article
  1. Abstract:

    We have identified a region related to the protease domain of bacterial and organelle ATP-dependent Lon proteases in virus protein 4 (VP4) of infectious bursal disease virus strain P2 (IBDVP2), a two-segmented double-stranded RNA virus, Unlike canonical Lens, IBDVP2 VP4 possesses a proteinase activity though it lacks an ATPase domain. Ser652 and Lvs692 of IBDVP2 VP4 are conserved across the Lon/VP4 family and are essential for catalysis, Lys692 has the properties of a general base, increasing the nucleophilicity of Ser652; a similar catalytic dyad may function in the other Lens, VP4 can cleave in trails and is responsible for the interdomain proteolytic autoprocessing of the QVP2-VP4-VP3 polyprotein encoded by RNA segment A. VP2, which is later derived from pVP2, and VP3 are major capsid proteins of birnaviruses, Results of the characterization of a range of the IBDVP2 VP4 mutants in cell cultures implicate VP4 in trails-activation of the synthesis of VP1, putative RNA-dependent RNA polymerase encoded by RNA segment B, and in cleavage rate-dependent control of process(es) crucial for the generation of the infectious virus progeny. [References: 77]

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