4c53

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Crystal Structure of Guanarito virus GP2 in the post-fusion conformationCrystal Structure of Guanarito virus GP2 in the post-fusion conformation

Structural highlights

4c53 is a 3 chain structure with sequence from Guanarito mammarenavirus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 4.14Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GLYC_GTOVV Interacts with the host receptor (By similarity). Mediates virus attachment to host TFRC. This attachment induces virion internalization predominantly through clathrin-mediated endocytosis (PubMed:17287727).[HAMAP-Rule:MF_04084][1] Class I viral fusion protein that directs fusion of viral and host endosomal membranes, leading to delivery of the nucleocapsid into the cytoplasm. Membrane fusion is mediated by irreversible conformational changes induced upon acidification in the endosome.[HAMAP-Rule:MF_04084] Stable signal peptide (SSP): cleaved and functions as a signal peptide. In addition, it is also retained as the third component of the GP complex. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of GP1 and GP2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion.[HAMAP-Rule:MF_04084]

Publication Abstract from PubMed

Guanarito virus (GTOV) is an emergent and deadly pathogen. We present the crystal structure of the glycosylated GTOV fusion glycoprotein to 4.1 A-resolution, in the post-fusion conformation. Our structure reveals a classical six-helix bundle and presents direct verification that New World arenaviruses exhibit class-I viral membrane fusion machinery. The structure provides visualization of an N-linked glycocalyx coat and consideration of glycan dynamics reveals extensive coverage of the underlying protein surface, following virus-host membrane fusion.

Crystal structure of Venezuelan hemorrhagic fever virus fusion glycoprotein reveals a class 1 post-fusion architecture with extensive glycosylation.,Parsy ML, Harlos K, Huiskonen JT, Bowden TA J Virol. 2013 Sep 18. PMID:24049182[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Radoshitzky SR, Abraham J, Spiropoulou CF, Kuhn JH, Nguyen D, Li W, Nagel J, Schmidt PJ, Nunberg JH, Andrews NC, Farzan M, Choe H. Transferrin receptor 1 is a cellular receptor for New World haemorrhagic fever arenaviruses. Nature. 2007 Mar 1;446(7131):92-6. Epub 2007 Feb 7. PMID:17287727 doi:http://dx.doi.org/10.1038/nature05539
  2. Parsy ML, Harlos K, Huiskonen JT, Bowden TA. Crystal structure of Venezuelan hemorrhagic fever virus fusion glycoprotein reveals a class 1 post-fusion architecture with extensive glycosylation. J Virol. 2013 Sep 18. PMID:24049182 doi:10.1128/JVI.02298-13

4c53, resolution 4.14Å

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