Proteolytic Processing and Particle Maturation

  • V. M. Vogt
Part of the Current Topics in Microbiology and Immunology book series (CT MICROBIOLOGY, volume 214)

Abstract

Proteolytic processing of the structural and enzymatic proteins of viruses is a common phenomenon (Krausslich and Wimmer 1988; Dougherty and Semler 1993). Well-studied examples include picornaviruses (such as poliovirus), alphaviruses (such as Sindbis virus), adenoviruses, plant viruses (such as potyviruses), and bacteriophage (such as T4). Cleavages of viral polypeptides have diverse functions, but they can be viewed most simply as serving to drive a reaction in one direction, since hydrolysis of the peptide bond in most situations is irreversible. In particular, cleavages often play roles in virion morphogenesis; in the most extreme cases complete degradation of a “scaffolding protein” is needed for the final infectious virus particle to be formed from an immature particle. In retroviruses all three major virion proteins, Gag, Pol, and Env, are proteolytically processed. For Gag and Pol it is the virus-encoded protease (PR) that accomplishes these cleavages, while for Env it is a host-encoded protease found in the Golgi apparatus. However, in some viruses the very C-terminus of Env also is processed by PR. In this chapter only PR-mediated processing is discussed, with a focus on the regulation of processing and the consequences of processing. Related topics such as PR structure, mechanism of catalysis, action of protease inhibitors, comparative aspects of retroviral proteases, and specificity of cleavage are treated perfunctorily. Many aspects of proteolytic processing in retroviruses have been reviewed elsewhere (Kráusslich and Wimmer 1988; Skalka 1989; Fitzgerald and Springer 1991; Wills and Craven 1991; Debouck 1992; Wlodawer and Erickson 1993; Katz and Skalka 1994; Ringe 1994; Tomasselli and Heindrikson 1994).

Keywords

Hydrolysis Toxicity Codon Amide Influenza 

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Copyright information

© Springer-Verlag Berlin Heidelberg 1996

Authors and Affiliations

  • V. M. Vogt
    • 1
  1. 1.Section of Biochemistry, Molecular and Cell Biology, Biotechnology BuildingCornell UniversityIthacaUSA

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