Identification, Characterization, and In Vitro Culture of Highly Divergent Arenaviruses from Boa Constrictors and Annulated Tree Boas: Candidate Etiological Agents for Snake Inclusion Body Disease

Stenglein, Mark D.; Sanders, Chris; Kistler, Amy L.; Ruby, J. Graham; Franco, Jessica Y.; Reavill, Drury R.; Dunker, Freeland; DeRisi, Joseph L.

Arenavirus Z proteins are essential for virus budding and are myristoylated on the amino (N) terminus (30) (31) (32) . The snake virus Z proteins do not possess N-terminal glycine residues typically associated with myristoylation but instead have predicted transmembrane domains in their first 50 amino acids, which may serve a similar role. Most arenavirus Z proteins also contain carboxyl (C)-terminal "late" domains with characteristic motifs (commonly PTAP or PPPY) that recruit cellular proteins that help drive virus budding (33) . The CASV and GGV Z proteins do not contain recognizable late domain motifs in their C termini. However, the C-terminal sequences of the NPs of these viruses do contain short motifs similar to late motifs (PKPV and PTPA), and it is possible that, as is the case for Marburg virus, NP contains a functional late domain (34) .