Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural transitions in influenza haemagglutinin at membrane fusion pH.
Journal, issue, pages	Nature, Vol. 583, Issue 7814, Page 150-153, Year 2020
Publish date	May 27, 2020
Authors	Donald J Benton / Steven J Gamblin / Peter B Rosenthal / John J Skehel /
PubMed Abstract	Infection by enveloped viruses involves fusion of their lipid envelopes with cellular membranes to release the viral genome into cells. For HIV, Ebola, influenza and numerous other viruses, envelope ...Infection by enveloped viruses involves fusion of their lipid envelopes with cellular membranes to release the viral genome into cells. For HIV, Ebola, influenza and numerous other viruses, envelope glycoproteins bind the infecting virion to cell-surface receptors and mediate membrane fusion. In the case of influenza, the receptor-binding glycoprotein is the haemagglutinin (HA), and following receptor-mediated uptake of the bound virus by endocytosis, it is the HA that mediates fusion of the virus envelope with the membrane of the endosome. Each subunit of the trimeric HA consists of two disulfide-linked polypeptides, HA1 and HA2. The larger, virus-membrane-distal, HA1 mediates receptor binding; the smaller, membrane-proximal, HA2 anchors HA in the envelope and contains the fusion peptide, a region that is directly involved in membrane interaction. The low pH of endosomes activates fusion by facilitating irreversible conformational changes in the glycoprotein. The structures of the initial HA at neutral pH and the final HA at fusion pH have been investigated by electron microscopy and X-ray crystallography. Here, to further study the process of fusion, we incubate HA for different times at pH 5.0 and directly image structural changes using single-particle cryo-electron microscopy. We describe three distinct, previously undescribed forms of HA, most notably a 150 Å-long triple-helical coil of HA2, which may bridge between the viral and endosomal membranes. Comparison of these structures reveals concerted conformational rearrangements through which the HA mediates membrane fusion.
External links	Nature / PubMed:32461688 / PubMed Central
Methods	EM (single particle)
Resolution	3.0 - 9.9 Å
Structure data	10696 6y5g EMDB-10696, PDB-6y5g: Ectodomain of X-31 Haemagglutinin at pH 8 Method: EM (single particle) / Resolution: 3.0 Å 10697 6y5h EMDB-10697, PDB-6y5h: Ectodomain of X-31 Haemagglutinin at pH 5 (State I) Method: EM (single particle) / Resolution: 3.0 Å 10698 6y5i EMDB-10698, PDB-6y5i: Dilated form 1 of X-31 Influenza Haemagglutinin at pH 5 (State II) Method: EM (single particle) / Resolution: 5.5 Å 10699 6y5j EMDB-10699, PDB-6y5j: Dilated form 2 of X-31 Influenza Haemagglutinin at pH 5 (State III) Method: EM (single particle) / Resolution: 5.6 Å 10700 6y5k EMDB-10700, PDB-6y5k: Extended Intermediate form of X-31 Influenza Haemagglutinin at pH 5 (State IV) Method: EM (single particle) / Resolution: 4.2 Å 10701 6y5l EMDB-10701, PDB-6y5l: Signal Subtracted Extended Intermediate form of X-31 Influenza Haemagglutinin at pH 5 (State IV) Method: EM (single particle) / Resolution: 3.6 Å EMDB-10702: Post-fusion X-31 Influenza Haemagglutinin at pH 5 (State V) Method: EM (single particle) / Resolution: 9.9 Å
Chemicals	ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine
Source	unidentified influenza virus unidentified influenza virus
Keywords	VIRAL PROTEIN / Haemagglutinin / Hemagglutinin / Fusion protein