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Journal of Virology, December 2009, p. 12651-12655, Vol. 83, No. 23
0022-538X/09/$08.00+0     doi:10.1128/JVI.01012-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

The Z Protein of the New World Arenavirus Tacaribe Virus Has Bona Fide Budding Activity That Does Not Depend on Known Late Domain Motifs{triangledown}

Shuzo Urata,1 Jiro Yasuda,2 and Juan Carlos de la Torre1*

Department of Immunology and Microbial Science, IMM-6, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037,1 First Department of Forensic Science, National Research Institute of Police Science, Kashiwa 277-0882, Japan2

Received 19 May 2009/ Accepted 3 September 2009

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.

* Corresponding author. Mailing address: Department of Immunology and Microbial Science, The Scripps Research Institute, 10550 North Torrey Pines Road, IMM-6, La Jolla, CA 92037. Phone: (858) 784-9462. Fax: (858) 784-9981. E-mail: juanct{at}scripps.edu

{triangledown} Published ahead of print on 16 September 2009.

Journal of Virology, December 2009, p. 12651-12655, Vol. 83, No. 23
0022-538X/09/$08.00+0     doi:10.1128/JVI.01012-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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