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Nat Struct Mol Biol. 2016 Jun;23(6):513-521. doi: 10.1038/nsmb.3210. Epub 2016 Apr 25.

Crystal structure of the prefusion surface glycoprotein of the prototypic arenavirus LCMV.

Author information

1
Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, CA, USA.
2
SOLEIL Synchrotron, Gif-sur-Yvette, France.
3
Department of Pediatrics, School of Medicine, Tulane University, New Orleans, LA, USA.
4
Department of Microbiology and Immunology, Tulane University, New Orleans, LA, USA.
5
Département de Virologie, Unité de Virologie Structurale, Institut Pasteur, Paris, France.
6
Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA, USA.
#
Contributed equally

Abstract

Arenaviruses exist worldwide and can cause hemorrhagic fever and neurologic disease. A single glycoprotein expressed on the viral surface mediates entry into target cells. This glycoprotein, termed GPC, contains a membrane-associated signal peptide, a receptor-binding subunit termed GP1 and a fusion-mediating subunit termed GP2. Although GPC is a critical target of antibodies and vaccines, the structure of the metastable GP1-GP2 prefusion complex has remained elusive for all arenaviruses. Here we describe the crystal structure of the fully glycosylated prefusion GP1-GP2 complex of the prototypic arenavirus LCMV at 3.5 Å. This structure reveals the conformational changes that the arenavirus glycoprotein must undergo to cause fusion and illustrates the fusion regions and potential oligomeric states.

PMID:
27111888
PMCID:
PMC4945123
DOI:
10.1038/nsmb.3210
[Indexed for MEDLINE]
Free PMC Article

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