The Z Protein of the New World Arenavirus Tacaribe Virus Has Bona Fide Budding Activity That Does Not Depend on Known Late Domain Motifs
Author(s) -
Shuzo Urata,
Jiro Yasuda,
Juan Carlos de la Torre
Publication year - 2009
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.01012-09
Subject(s) - arenavirus , budding , biology , tsg101 , junin virus , virology , protein domain , lymphocytic choriomeningitis , microbiology and biotechnology , genetics , gene , microrna , in vitro , microvesicles , cytotoxic t cell
The arenavirus small RING finger Z protein has been shown to be the main driving force of budding for several arenaviruses. This Z budding activity was found to be mediated by the late (L)-domain motifs P(T/S)AP and PPXY, located at the C terminus of Z. Here, we show that the Z protein of Tacaribe virus (TACV), a New World arenavirus, buds efficiently from cells despite lacking the canonical L-domain motifs P(T/S)AP and PPXY. Likewise, potential L-domain motifs ASAP and YLCL present in TACV Z did not exhibit any significant contribution to TACV Z budding activity. Budding of TACV Z was Tsg101 independent but required the activity of Vps4A/B. These results indicate that TACV Z utilizes a budding mechanism distinct from that reported for other arenaviruses.
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