Mapping of the tacaribe arenavirus Z-protein binding sites on the L protein identified both amino acids within the putative polymerase domain and a region at the N terminus of L that are critically involved in binding.

Journal of Virology
Maximiliano WildaMaria T Franze-Fernandez


Tacaribe virus (TacV) is the prototype of the New World group of arenaviruses. The TacV genome encodes four proteins: the nucleoprotein (N), the glycoprotein precursor, the polymerase (L), and a RING finger protein (Z). Using a reverse genetics system, we demonstrated that TacV N and L are sufficient to drive transcription and replication mediated by TacV-like RNAs and that Z is a powerful inhibitor of these processes (Lopez et al., J. Virol. 65:12241-12251, 2001). More recently, we provided the first evidence of an interaction between Z and L and showed that Z's inhibitory activity was dependent on its ability to bind to L (Jácamo et al., J. Virol. 77:10383-10393, 2003). In the present study, we mapped the TacV Z-binding sites on the 2,210-amino-acid L polymerase. To that end, we performed deletion analysis and point mutations of L and studied the Z-L interaction by coimmunoprecipitation with specific sera. We found that the C-terminal region of L was not essential for the interaction and identified two noncontiguous regions that were critical for binding: one at the N-terminus of L between residues 156 and 292 and a second one in the polymerase domain (domain III). The importance of domain III in binding was revealed by subst...Continue Reading


Jan 1, 1987·Current Topics in Microbiology and Immunology·D H Bishop, D D Auperin
Nov 1, 1986·Proceedings of the National Academy of Sciences of the United States of America·T R FuerstB Moss
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Sep 13, 2003·Journal of Virology·Rodrigo JácamoMaría T Franze-Fernández
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Feb 20, 2004·Virology·Simon ViethStephan Günther
Mar 3, 2004·Journal of Virology·Tatjana I CornuJuan Carlos de la Torre

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