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https://bar.utoronto.ca/thalemine/service/ is incorrect| Description | Arenaviridae are single stranded RNA viruses. The arenaviridae S RNAs that have been characterised include conserved terminal sequences, an ambisense arrangement of the coding regions for the precursor glycoprotein (GPC) and nucleocapsid (N) proteins and an intergenic region capable of forming a base-paired "hairpin"structure. The mature glycoproteins that result are G1 and G2 and the N protein [ ].Tacaribe virus (TACV) is an arenavirus that is genetically and antigenically closely related to Junin arenavirus (JUNV), the aetiological agent of Argentine haemorrhagic fever (AHF). It is well established that TACV protects experimental animals fully against an otherwise lethal challenge with JUNV. It has been established that it is the heterologous glycoprotein that protects against JUNV challenge. A recombinant vaccinia virus that expresses JUNV glycoprotein precursor (VV-GJun) protected seventy-two percent of the animals inoculated with two doses of VV-GJun against the lethal JUNV challenge [ ].The GPC complex contains a cleaved stable signal peptide (SSP) in addition to the canonical receptor-binding (G1) and transmembrane fusion (G2) subunits. SSP is essential for intracellular transport of the GPC complex to the cell surface and for its membrane-fusion activity.This superfamily represents the zinc binding domain of GPC, available data is derived from studies on Junin arenavirus (JUNV). The face of the domain that contains the two zinc-binding clusters is well conserved among arenaviruses, and cluster II serves as a binding site for Cys-57 in the SSP. It is believed that the zinc-mediated anchoring of SSP contributes to positioning the ectodomain loop of SSP relative to the G2 ectodomain to modulate membrane fusion [ ]. | Name | Arenavirus glycoprotein, zinc binding domain |
| Short Name | Arena_glycoprot_zinc-bd | Type | Homologous_superfamily |
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