Importance
Lassa virus, an Old World arenavirus, is a notorious disease-causing agent primarily in West Africa that is able to spread to rodents, as well as humans. This deadly pathogen causes severe viral hemorrhagic fevers and significant mortality. So far, there are no available vaccines for Lassa virus or any other viruses found in the Arenaviridae family. Determining the structure of the complete trimeric glycoprotein complex, composed of GP1, GP2, and SSP (stable signal peptide), will lay the foundation for a future discovery of novel antiviral drugs. This is the first representative structure for Old World arenaviruses.
Function
GP1 (Glycoprotein 1) is the receptor binding domain of Lassa virus that mediates receptor recognition.
Structural Highlights
Protein structure accession number: 4ZJF. 4ZJF is a 4 chain structure with ligands attached to each chain. The overall architecture of GP1 features a central β-sheet and two distinct halves: a glycosylated half containing the receptor-binding site that is made mostly by the central β-sheet and surrounding loops and a half that contains mostly helices and most likely faces the trimer axis[1]..
For more information on this protein structure visit the following sites: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT
Histidine Triad
Attached to this structure is a that is highly conserved among Old World arenaviruses. The histidine triad is a structural element that directly interacts with LAMP1 and helps stabilize a LAMP1-"compatible" conformation by providing a molecular mechanism for the pH-dependent receptor switching[1].
