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6ZJM

Atomic model of Andes virus glycoprotein spike tetramer generated by fitting into a Tula virus reconstruction

Summary for 6ZJM
Entry DOI10.2210/pdb6zjm/pdb
EMDB information11236
DescriptorEnvelope polyprotein,Envelope polyprotein,Envelope polyprotein,Envelope polyprotein,Envelope polyprotein,Envelope polyprotein,Envelope polyprotein,Envelope polyprotein,Envelope polyprotein, alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
Functional Keywordshantavirus, tula, andes, tulv, andv, glycoprotein, lattice, spike, fusion protein, viral protein
Biological sourceTula orthohantavirus
More
Total number of polymer chains8
Total formula weight909271.17
Authors
Stass, R.,Huiskonen, J.T.,Rey, F.,Guardado-Calvo, P. (deposition date: 2020-06-29, release date: 2020-10-14, Last modification date: 2024-11-06)
Primary citationSerris, A.,Stass, R.,Bignon, E.A.,Muena, N.A.,Manuguerra, J.C.,Jangra, R.K.,Li, S.,Chandran, K.,Tischler, N.D.,Huiskonen, J.T.,Rey, F.A.,Guardado-Calvo, P.
The Hantavirus Surface Glycoprotein Lattice and Its Fusion Control Mechanism.
Cell, 183:442-, 2020
Cited by
PubMed Abstract: Hantaviruses are rodent-borne viruses causing serious zoonotic outbreaks worldwide for which no treatment is available. Hantavirus particles are pleomorphic and display a characteristic square surface lattice. The envelope glycoproteins Gn and Gc form heterodimers that further assemble into tetrameric spikes, the lattice building blocks. The glycoproteins, which are the sole targets of neutralizing antibodies, drive virus entry via receptor-mediated endocytosis and endosomal membrane fusion. Here we describe the high-resolution X-ray structures of the heterodimer of Gc and the Gn head and of the homotetrameric Gn base. Docking them into an 11.4-Å-resolution cryoelectron tomography map of the hantavirus surface accounted for the complete extramembrane portion of the viral glycoprotein shell and allowed a detailed description of the surface organization of these pleomorphic virions. Our results, which further revealed a built-in mechanism controlling Gc membrane insertion for fusion, pave the way for immunogen design to protect against pathogenic hantaviruses.
PubMed: 32937107
DOI: 10.1016/j.cell.2020.08.023
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (11.4 Å)
Structure validation

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数据于2025-10-22公开中

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