{"database":"bioimages","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Sonia Libersou"],"journal":["The Journal of Cell Biology"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-JCBD-201006116"],"attach_to":["JCB"],"legend":["A) After incubation for 15 minutes at pH 6.6 and 37°C, virions are not aggregated and most of the spikes are in their post-fusion conformation (ectodomain length of 12 nm). B) The viral preparation shown in A) was subsequently incubated at pH 6.0 and 20°C for 20 minutes. All the spikes are in their post-fusion conformation and the virions have retained their initial shape. The arrow indicates a virion with its surface completely covered by spikes in their post-fusion conformation. C-G) The viral preparation shown in A) was subsequently incubated at pH 5.5 and 20°C for 20 minutes. Most of the particles are disrupted. Extensive lattices of G are visible at the surface of the virion (arrows in C, disrupted virion in D). In many cases (E, F, G), the particles are highly damaged, precluding the","(A) At pH 7.5, VSV formed a monodisperse suspension with virions that were bullet-shaped when viewed from the side and circular when viewed from above. The asterisks indicate viruses with a base depleted of glycoproteins. (B) Higher magnification of the virions indicated by an arrow in A. Continuous layer of G over the surface of the virus (large arrow), with a lower density at the base of the particle (thin arrows). The right arrow indicates a virus with no spikes visible at its base. (C) VSV forms large aggregates at pH 6.0. G has a more elongated structure, making it possible to distinguish individual spikes, which are often closely packed at the apex of the viral particle (arrows). (D) At pH 5.5, the spikes form ordered helical arrays. Note that the viral particles fuse at their bases.","(A) At pH 7.5, viral particles and liposomes do not fuse. (B) At pH 6.0, G shows the characteristic post-fusion conformation and numerous fusion events are observed. (C) At pH 5.5, individual fusion events can be seen. Fusion proceeds from the base of the virus, and G forms helical arrays on the cylindrical part of the viral particle.","(A,B) Three sections of the tomograms are shown (extracted from movies S1 and S3); one at the level of the G layer (left frame), one at the level of the nucleocapsid (middle frame) and one passing through the center of the particle (right frame). The tilted series used to calculate the tomograms were recorded on negatively stained samples. (A) At pH 7.5, VSV is bullet-shaped, with a central cavity. In some areas, the G layer contains trimeric entities (arrows in the enlargement). As the stain does not penetrate the viral particle, the nucleocapsids are not visible. (B) At pH 5.5, G shows trimeric structures that form quasi-helical arrays (left frame). The nucleocapsid is now visible (middle and right frames). In the center of the particle, a twisted material occupies the central cavity. (C","A) At pH 6, Gth , inserted into liposomes that were initially spherical, forms a local network (indicated by the arrow and enlarged in the upper right frame), favoring the formation of tubular structures. B) At pH 5.5, Gth forms more extensive, regular arrays at the surface of liposomes, resembling those formed by G at the surface of the virus. Spherical vesicles are nevertheless still visible (arrow). C) At pH 5.2, only rigid tubular protein-lipid structures are observed, at the surface of which Gth displays quasi-helical symmetry. <br />All the samples were negatively stained for electron microscopy observation.<br /><br />","(A) At pH 7.5, some viral particles interact with liposomes, but no fusion is detected. (B) At pH 6.0, viral particles and liposomes aggregate and numerous fusion events are visible. Fusion events are characterized by the presence of several nucleocapsids within a liposome, the membrane of which contains glycoproteins in the post-fusion conformation, often clustered into locally ordered arrays (arrow; the magnified area is inserted). (C) At pH 5.5, individual fusion events can be seen, demonstrating that fusion occurs at the base of the virion and that spikes located on the cylindrical part of the virus form ordered helical arrays.","(A) At pH 7.5, G forms a thin continuous layer around the viral particle. The arrows indicate viruses with no G visible at their base. (B) At pH 6, G elongates and individual spikes protruding from the membrane are visible. The arrow indicates an area in which the spikes are regularly organized. (C) At pH 5.5, all the spikes display a well ordered helical organization. Note that the membrane at the base of the particle is disrupted, allowing the release of internal material (indicated by arrows). In A and B, the image is underfocused by about 1.8 µm. In C, it is underfocused by 3 µm, to improve visualization of the helical G array."],"repository":["bioimages"],"figure_sub":["Image 23653 (Figure 6 - None)","Figure 6 - None","Image 23656 (Figure 8 - None)","Figure 2 - None","Figure 3 - None","Figure 4 - None","Figure 5 - None","Figure 7 - None","Image 23657 (Figure 2 - None)","Image 23654 (Figure 7 - None)","Image 23659 (Figure 4 - None)","Figure 5","Figure 4","Image 23643 (Figure 3 - None)","Image 23652 (Figure 5 - None)","Figure 7","Figure 6","Figure 8","Figure 8 - None","Figure 3","Figure 2"],"pubmed_authors":["Malika Ouldali","Yves Gaudin","Hélène Raux","Aurélie A.V. Albertini","Christine Maheu","Stéphane Roche","Felix de Haas","Jean Lepault","Virginie Maury","Sonia Libersou"],"additional_accession":[]},"is_claimable":false,"name":"Distinct structural rearrangements of the VSV glycoprotein drive membrane fusion","description":null,"dates":{"release":"2010-10-04T11:20:45Z","modification":"2018-11-29T11:20:45Z","creation":"2018-11-29T11:20:45Z"},"accession":"S-JCBD-201006116","cross_references":{"doi":["10.1083/jcb.201006116"]}}