Arenavirus budding resulting from viral-protein-associated cell membrane curvature

Schley, David; Whittaker, Robert J.; Neuman, Benjamin W.

doi:10.1098/rsif.2013.0403

Cited by 11 publications

(10 citation statements)

References 74 publications

(87 reference statements)

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“…In the limit of an endosome that is much larger than the ILV, as is the case in this system, the pressure that acts across the lipid bilayer causes an effective far field tension, with σ the surface tension coefficient [53]. This means that remodeling the membrane away from a flat shape requires a surface energy ∆Eσ…”

Section: Resultsmentioning

confidence: 96%

Protein Crowding Mediates Membrane Remodeling in Upstream ESCRT-induced Formation of Intraluminal Vesicles

Liese

Wenzel

Kjos

et al. 2019

Preprint

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AbstractAs part of the lysosomal degradation pathway, the endosomal sorting complexes required for transport (ESCRT-0-III/VPS4) sequester receptors at the endosome and simultaneously deform the membrane to generate intraluminal vesicles (ILVs). Whereas ESCRT-III/VPS4 have an established function in ILV formation, the role of upstream ESCRTs (0-II) in membrane shape remodeling is not understood. Combining experimental measurements and electron microscopy analysis of ESCRT-III depleted cells with a mathematical model, we show that upstream ESCRT-induced alteration of the Gaussian bending rigidity and their crowding on the membrane induces membrane deformation and facilitates ILV formation: upstream ESCRT-driven budding does not require ATP consumption as only a small energy barrier needs to be overcome. Our model predicts that ESCRTs do not become part of the ILV, but localize with a high density at the membrane neck, where the steep decline in the Gaussian curvature likely triggers ESCRT-III/VPS4 assembly to enable neck constriction and scission.Significance StatementIntraluminal vesicle (ILV) formation plays a crucial role in the attenuation of growth factor receptor signaling, which is mediated by the endosomal sorting complex required for transport (ESCRT-0-III/VPS4). The general dogma has been that the upstream ESCRTs (0-II) sequester the receptors at the surface of endosomes and the downstream ESCRTs (III/VPS4) remodel the endosome membrane leading to the abscission and formation of receptor-containing ILVs. We now show that the upstream ESCRTs not only sequester cargo, but in addition play an essential role for the initiation of membrane shape remodeling in ILV budding. Through a combination of mathematical modeling and experimental measurements we show that upstream ESCRTs facilitate ILV budding by crowding with a high density in the membrane neck region.

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Section: Resultsmentioning

confidence: 96%

Protein Crowding Mediates Membrane Remodeling in Upstream ESCRT-induced Formation of Intraluminal Vesicles

Liese

Wenzel

Kjos

et al. 2019

Preprint

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“…Arenavirus Z protein is a key factor in virus budding and is sufficient for the release of virus-like particles (VLPs). This activity is mediated by late (L) domain motifs, PT/SAP and PPXY, located at the Cterminus of Z (Schley et al, 2013;. LASV Z protein efficiently produces VLPs and, as other RNA viruses, uses MVB pathway (Vsp4A, Vps4B, and Tsg101) to facilitate budding process (Urata et al, 2006).…”

Section: Transcription Replication and Synthesis Of Viral Proteinsmentioning

confidence: 99%

Pathogenesis of Helicobacter pylori in Humans

Zambon

Basso

Pelloso

et al. 2015

Human Emerging and Re‐emerging Infections

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The Old World arenaviruses: taxonomic and zoonotic introduction Arenaviruses represent a fast-growing group of rodent-borne viruses (see Notes in the Proofs) which are an example of how environmental changes disrupt the natural animal virus-host balance and result in unexpected diseases. In the wild, arenaviruses exist as chronic infections in specific rodent hosts. This provides ideal conditions for competition within viral quasispecies for improved adaptation to the host. Analysis of arenavirus phylogeny and rodent cytochrome-b sequences provides examples of coevolution of arenaviruses with their rodent hosts. Based on their antigenic properties and geographic distribution approximately two dozen arenaviruses discovered so far are placed into two groups: the Old World (OW) or Lassa-LCMV complex and the New World (NW) or Tacaribe complex (Salvato et al., 2012). In general, the OW viruses are hosted by rodents of the family Muridae, subfamily Murinae. The NW arenaviruses are associated with rodents of the subfamily Sigmodontinae which are divided into the North and South American lineages. Phylogenetically the NW arenaviruses are further divided into clades A, B, C, and a recombinant A/B clade. Lymphocytic choriomeningitis virus (LCMV), the prototypic arenavirus that belongs to the OW group, is hosted by the house mouse (Mus musculus). The virus is distributed worldwide and can cause aseptic meningitis or meningoencephalitis in immunocompetent children and adults. Recent studies indicate that LCMV is also an under-recognized cause of congenital infection and neurological disease in the fetus and newborns (Bonthius, 2012; Laposova

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“…TM domains that feature conical shapes, as a product of this shape, will induce membrane curvature by forcing the membrane to accommodate and deform around the conical region in a wedge-like manner (McMahon and Gallop, 2005;Shibata et al, 2009). Additionally, suites of proteins may form together as a scaffold that has the ability to deform lipid bilayers and steric effects of these membrane-interacting proteins may also aid in deformation (Schley et al, 2013). Since nsp3, nsp4, and nsp6 (and their Nidovirales homologs) contain TM domains and work together in a scaffold-like fashion, it is possible that both of these approaches work together to induce DMVs and CMs.…”

Section: Theoretical Mechanismmentioning

confidence: 99%