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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
Author(s) -
Calistri Arianna,
Del Vecchio Claudia,
Salata Cristiano,
Celestino Michele,
Celegato Marta,
Göttlinger Heinrich,
Palù Giorgio,
Parolin Cristina
Publication year - 2009
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.21587
Subject(s) - feline immunodeficiency virus , nedd4 , ubiquitin ligase , ubiquitin , biology , microbiology and biotechnology , virology , biogenesis , viral protein , lentivirus , virus , genetics , viral disease , gene
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 a functional 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. J. Cell. Physiol. 218: 175–182, 2009. © 2008 Wiley‐Liss, Inc.