The z protein of the new world arenavirus tacaribe virus has bona fide budding activity that does not depend on known late domain motifs.
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.
Urata
Shuzo
S
Department of Immunology and Microbial Science, IMM-6, The Scripps Research Institute, La Jolla, California 92037, USA.
Yasuda
Jiro
J
de la Torre
Juan Carlos
JC
D020816:Amino Acid Motifs; D006477:Arenaviruses, New World / Q000235:genetics / Q000502:physiology*; D006801:Humans; D017434:Protein Structure, Tertiary; D014764:Viral Proteins / Q000235:genetics / Q000502:physiology*; D014779:Virus Replication
D014764:Viral Proteins