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  • The proteosomal degradation of fusion proteins cannot be predicted from the proteosome susceptibility of their individual components

    Author(s)
    O. Ilyinskii, Petr
    B. Meriin, Anatoli
    L. Gabai, Vladimir
    V. Usachev, Evgeny
    G. Prilipov, Alexei
    Thoidis, Galini
    M. Schnieder, Alexander
    Griffith University Author(s)
    Usachev, Evgeny
    Year published
    2008
    Metadata
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    Abstract
    It is assumed that the proteosome-processing characteristics of fusion constructs can be predicted from the sum of the proteosome sensitivity of their components. In the present study, we observed that a fusion construct consisting of proteosome-degradable proteins does not necessarily result in a proteosomedegradable chimera. Conversely, fusion of proteosome-resistant proteins may result in a proteosomedegradable composite. We previously demonstrated that conserved influenza proteins can be unified into a single fusion antigen that is protective, and that vaccination with combinations of proteosome-resistant and ...
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    It is assumed that the proteosome-processing characteristics of fusion constructs can be predicted from the sum of the proteosome sensitivity of their components. In the present study, we observed that a fusion construct consisting of proteosome-degradable proteins does not necessarily result in a proteosomedegradable chimera. Conversely, fusion of proteosome-resistant proteins may result in a proteosomedegradable composite. We previously demonstrated that conserved influenza proteins can be unified into a single fusion antigen that is protective, and that vaccination with combinations of proteosome-resistant and proteosome-degradable antigens resulted in an augmented T-cell response. In the present study we constructed proteosome-degradable mutants of conserved influenza proteins NP, M1, NS1, and M2. These were then fused into multipartite proteins in different positions. The stability and degradation profiles of these fusion constructs were demonstrated to depend on the relative position of the individual proteins within the chimeric molecule. Combining unstable sequences of either NP and M1 or NS1 and M2 resulted in either rapidly proteosome degraded or proteosome-resistant bipartite fusion mutants. However, further unification of the proteosome-degradable forms into a single four-partite fusion molecule resulted in relatively stable chimeric proteins. Conversely, the addition of proteosome-resistant wild-type M2 to proteosomeresistant NP-M1-NS1 fusion protein lead to the decreased stability of the resulting four-partite multigene products, which in one case was clearly proteosome dependent. Additionally, a highly destabilized form of M1 failed to destabilize the wild-type NP. Collectively, we did not observe any additive effect leading to proteosomal degradation/nondegradation of a multigene construct.
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    Journal Title
    Protein Science
    Volume
    17
    Issue
    6
    DOI
    https://doi.org/10.1110/ps.083443908
    Copyright Statement
    Self-archiving of the author-manuscript version is not yet supported by this journal. Please refer to the journal link for access to the definitive, published version or contact the author[s] for more information.
    Subject
    Biochemistry and Cell Biology not elsewhere classified
    Biochemistry and Cell Biology
    Computation Theory and Mathematics
    Other Information and Computing Sciences
    Publication URI
    http://hdl.handle.net/10072/32042
    Collection
    • Journal articles

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