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Related Experiment Videos

Molecular processing of adenovirus proteins.

M T Sung, T M Cao, M A Lischwe

    The Journal of Biological Chemistry
    |July 10, 1983
    PubMed
    Summary

    Adenovirus protease processes viral proteins for infectivity. A common Gly-Gly-Ala sequence in precursors Pro-VI and Pro-VII suggests a shared mechanism for viral assembly.

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    Area of Science:

    • Virology
    • Molecular Biology
    • Structural Biology

    Background:

    • Adenovirus infection involves virus-encoded protease activity crucial for viral maturation and infectivity.
    • Specific processing of viral structural proteins, like core protein VII, is a prerequisite for forming infectious virions.

    Purpose of the Study:

    • To elucidate the processing events of adenovirus core protein VII.
    • To investigate the substrate specificity of the viral endoprotease by examining Pro-VI.
    • To identify a consensus sequence and potential common mechanism for processing viral precursors.

    Main Methods:

    • Protein and nucleotide sequencing to determine the structure of the precursor peptide sequence for protein VII.
    • Isolation and characterization of another viral proprotein precursor, Pro-VI.
    • Comparison of propeptide sequences at cleavage sites.

    Main Results:

    • Two processing events for protein VII were identified: removal of initiator methionyl residue and acetylation of the penultimate seryl residue during biosynthesis, followed by removal of an N-terminal 23-residue fragment during assembly.
    • A consensus amino acid sequence (Gly-Gly-Ala) was identified at the cleavage site of both Pro-VI and Pro-VII.
    • Extensive similarity was observed in the precursor sequences of Pro-VI and Pro-VII.

    Conclusions:

    • The viral protease plays a critical role in adenovirus maturation by processing structural proteins.
    • The identified consensus sequence (Gly-Gly-Ala) suggests a specific recognition motif for the viral endoprotease.
    • The similarities between Pro-VI and Pro-VII processing indicate a common mechanism controlling the reorganization of these proteins during virion assembly.

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