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Lassa virus is an enveloped, bi-segmented RNA virus and the most prevalent and fatal of all Old World arenaviruses. Virus entry into the host cell is mediated by a tripartite surface spike complex, which is composed of two viral glycoprotein subunits, GP1 and GP2, and the stable signal peptide. Of these, GP1 binds to cellular receptors and GP2 catalyzes fusion between the viral envelope and the host cell membrane during endocytosis. The molecular structure of the spike and conformational rearrangements induced by low pH, prior to fusion, remain poorly understood. Here, we analyzed the three-dimensional ultrastructure of Lassa virus using electron cryotomography. Sub-tomogram averaging yielded a structure of the glycoprotein spike at 14-Å resolution. The spikes are trimeric, cover the virion envelope, and connect to the underlying matrix. Structural changes to the spike, following acidification, support a viral entry mechanism dependent on binding to the lysosome-resident receptor LAMP1 and further dissociation of the membrane-distal GP1 subunits.

Original publication

DOI

10.1371/journal.ppat.1005418

Type

Journal article

Journal

PLoS Pathog

Publication Date

02/2016

Volume

12

Keywords

Animals, Cercopithecus aethiops, Glycoproteins, Hydrogen-Ion Concentration, Lassa virus, Lysosome-Associated Membrane Glycoproteins, Models, Molecular, Molecular Conformation, Multiprotein Complexes, Protein Binding, Protein Sorting Signals, Protein Structure, Tertiary, Vero Cells, Viral Envelope Proteins, Virion, Virus Internalization