The z protein of the new world arenavirus tacaribe virus has bona fide budding activity that does not depend on known late domain motifs

J Virol. 2009 Dec;83(23):12651-5. doi: 10.1128/JVI.01012-09. Epub 2009 Sep 16.

Abstract

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Arenaviruses, New World / genetics
  • Arenaviruses, New World / physiology*
  • Humans
  • Protein Structure, Tertiary
  • Viral Proteins / genetics
  • Viral Proteins / physiology*
  • Virus Replication*

Substances

  • Viral Proteins