Role of the feline immunodeficiency virus L-Domain in the presence or absence of gag processing: Involvement of ubiquitin and nedd4-2s ligase in viral egress

Arianna Calistri, D. E L Claudia Vecchio, Cristiano Salata, Michele Celestino, Marta Celegato, Heinrich Göttlinger, Giorgio Palù, Cristina Parolin

Research output: Contribution to journalArticle

Abstract

RNA-enveloped viruses bud from infected cells by exploiting the multivesicular body (MVB) pathway. In this context, ubiquitination of structural viral proteins and their direct interaction with cellular factors involved in the MVB biogenesis through short proline rich regions, named late domains (L-domains), are crucial mechanisms. Here we report that, in contrast with the human immunodeficiency virus (HIV), the feline immunodeficiency virus (FIV), a non-primate lentivirus, is strictly dependent for its budding on a ''PSAP''-type L-domain, mapping in the carboxy-terminal region of Gag, irrespective of afunctional viral protease. Moreover, we provide evidence that FIV egress is related to Gag ubiquitination, that is, linked to the presence of an active L-domain. Finally, although FIV Gag does not contain a PPxY motif, we show that the Nedd4-2s ubiquitin ligase enhances FIV Gag ubiquitination and it is capable to rescue viral mutants lacking a functional L-domain. In conclusion, our data bring to light peculiar aspects of FIV egress, but we also demonstrate that a non-primate lentivirus shares with HIV-1 a novel mechanism of connection to the cellular budding machinery.

Original languageEnglish
Pages (from-to)175-182
Number of pages8
JournalJournal of Cellular Physiology
Volume218
Issue number1
DOIs
Publication statusPublished - Jan 2009

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Cell Biology
  • Physiology

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    Calistri, A., Vecchio, D. E. L. C., Salata, C., Celestino, M., Celegato, M., Göttlinger, H., Palù, G., & Parolin, C. (2009). Role of the feline immunodeficiency virus L-Domain in the presence or absence of gag processing: Involvement of ubiquitin and nedd4-2s ligase in viral egress. Journal of Cellular Physiology, 218(1), 175-182. https://doi.org/10.1002/jcp.21587