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Open AccessReview

The Foamy Virus Gag Proteins: What Makes Them Different?

by Erik Müllers 1,2
Department of Cell and Molecular Biology, Karolinska Institutet, SE-17177 Stockholm, Sweden
Institut für Virologie, Medizinische Fakultät "Carl Gustav Carus", Technische Universität Dresden, Fetscherstr. 74, 01307 Dresden, Germany
Viruses 2013, 5(4), 1023-1041;
Received: 25 January 2013 / Revised: 15 March 2013 / Accepted: 20 March 2013 / Published: 26 March 2013
(This article belongs to the Special Issue Recent Progress in Foamy Virus (FV) Research)
Gag proteins play an important role in many stages of the retroviral replication cycle. They orchestrate viral assembly, interact with numerous host cell proteins, engage in regulation of viral gene expression, and provide the main driving force for virus intracellular trafficking and budding. Foamy Viruses (FV), also known as spumaviruses, display a number of unique features among retroviruses. Many of these features can be attributed to their Gag proteins. FV Gag proteins lack characteristic orthoretroviral domains like membrane-binding domains (M domains), the major homology region (MHR), and the hallmark Cys-His motifs. In contrast, they contain several distinct domains such as the essential Gag-Env interaction domain and the glycine and arginine rich boxes (GR boxes). Furthermore, FV Gag only undergoes limited maturation and follows an unusual pathway for nuclear translocation. This review summarizes the known FV Gag domains and motifs and their functions. In particular, it provides an overview of the unique structural and functional properties that distinguish FV Gag proteins from orthoretroviral Gag proteins. View Full-Text
Keywords: Foamy Virus Gag; functional domains; virus assembly; GR box, nuclear localization Foamy Virus Gag; functional domains; virus assembly; GR box, nuclear localization
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Müllers, E. The Foamy Virus Gag Proteins: What Makes Them Different? Viruses 2013, 5, 1023-1041.

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