Structure of intracellular mature vaccinia virus observed by cryoelectron microscopy

Dubochet, Jacques; Adrian, Marc; Richter, Karsten; Garcés, Javier; Wittek, Riccardo

doi:10.1128/jvi.68.3.1935-1941.1994

Cited by 73 publications

(50 citation statements)

References 19 publications

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“…Emerging evidence suggests that membrane-proximal protein lattices may be characteristic of enveloped non-icosahedral viruses and may represent an alternative to icosahedral and helical symmetry in virion architecture. For example, cryo-EM and cryoelectron tomography have demonstrated that glycoprotein spikes in the poxvirus core envelope (13,22) and the envelope of hepatitis B virus (20) are hexagonally packed. Retroviral Env may be organized similarly: hexagonal arrays were described for human foamy virus (82), and loose hexagonal packing was noted for human immunodeficiency virus type 1 and simian immunodeficiency virus (89).…”

Section: Discussionmentioning

confidence: 99%

“…Previous reports have noted that surface protein lattices on enveloped virions become disordered with increasing time and temperature. For instance, lattices of Sendai M protein disappeared upon prolonged storage at 37°C (1), while deterioration of vaccinia virus core envelope lattices occurred more slowly during cold storage (22). The kinetics of coronavirus lattice disruption and effects on infectivity are unknown and will require further study.…”

Section: Discussionmentioning

confidence: 99%

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Supramolecular Architecture of Severe Acute Respiratory Syndrome Coronavirus Revealed by Electron Cryomicroscopy

Neuman¹,

Adair

Yoshioka

et al. 2006

J Virol

394

362

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Coronavirus particles are enveloped and pleomorphic and are thus refractory to crystallization and symmetry-assisted reconstruction. A novel methodology of single-particle image analysis was applied to selected virus features to obtain a detailed model of the oligomeric state and spatial relationships among viral structural proteins. Two-dimensional images of the S, M, and N structural proteins of severe acute respiratory syndrome coronavirus and two other coronaviruses were refined to a resolution of ϳ4 nm. Proteins near the viral membrane were arranged in overlapping lattices surrounding a disordered core. Trimeric glycoprotein spikes were in register with four underlying ribonucleoprotein densities. However, the spikes were dispensable for ribonucleoprotein lattice formation. The ribonucleoprotein particles displayed coiled shapes when released from the viral membrane. Our results contribute to the understanding of the assembly pathway used by coronaviruses and other pleomorphic viruses and provide the first detailed view of coronavirus ultrastructure.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Supramolecular Architecture of Severe Acute Respiratory Syndrome Coronavirus Revealed by Electron Cryomicroscopy

Neuman¹,

Adair

Yoshioka

et al. 2006

J Virol

394

362

View full text Add to dashboard Cite

show abstract

“…Not depicted are corroborative DEEM images we have obtained of purified vaccinia virus cores generated by detergent extraction of isolated IMVs, in which case the lateral bodies are retained on the surface of the cores and thus are fully exposed and immediately apparent. They are clearly not an artifact, as one group once claimed (Dubochet et al, 1994).…”

Section: Cross Fractures Of Viral Coresmentioning

confidence: 93%

“…Moreover, we should have expected to see some sort of pattern of intramembrane particles on its fracture faces, if it had existed. This is because several earlier EM studies have shown that the clear zone around the core of IMVs is punctuated by a very distinctive array of "spicules", which has lead to its having been named the palisade layer (Easterbrook, 1966;Muller and Williamson, 1987;Dubochet et al, 1994). Such a palisade would surely be expected to yield some sort of regular pattern of intramembrane particles on the fracture face of the membrane to which it attached (again, if such a membrane existed).…”

Section: Deeper Cross Fractures Into Imvsmentioning

confidence: 99%

Deep-etch EM reveals that the early poxvirus envelope is a single membrane bilayer stabilized by a geodetic “honeycomb” surface coat

Heuser

2005

The Journal of Cell Biology

100

137

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Three-dimensional “deep-etch” electron microscopy (DEEM) resolves a longstanding controversy concerning poxvirus morphogenesis. By avoiding fixative-induced membrane distortions that confounded earlier studies, DEEM shows that the primary poxvirus envelope is a single membrane bilayer coated on its external surface by a continuous honeycomb lattice. Freeze fracture of quick-frozen poxvirus-infected cells further shows that there is only one fracture plane through this primary envelope, confirming that it consists of a single lipid bilayer. DEEM also illustrates that the honeycomb coating on this envelope is completely replaced by a different paracrystalline coat as the poxvirus matures. Correlative thin section images of infected cells freeze substituted after quick-freezing, plus DEEM imaging of Tokuyasu-type cryo-thin sections of infected cells (a new application introduced here) all indicate that the honeycomb network on immature poxvirus virions is sufficiently continuous and organized, and tightly associated with the envelope throughout development, to explain how its single lipid bilayer could remain stable in the cytoplasm even before it closes into a complete sphere.

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“…However, fine, well-preserved details on the surface of viruses were appreciated only in Ta replicas. The reason for this is that although negative staining is a very useful method that provides medium resolution when dealing with non-enveloped viruses and macromolecular complexes, it can be too disrupting for non-fixed membranous structures, such as viral envelopes (Dubochet et al, 1994;Harris and Scheffler, 2002;Kiselev et al, 1990).…”

Section: Resultsmentioning

confidence: 99%

Studying cellular architecture in three dimensions with improved resolution: Ta replicas revisited

Cabezas

Risco

2006

Cell Biology International

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Metal replicas have been used for surface analysis of biological structures with a variety of spatial resolutions. Platinum (Pt) has been the metal of choice because it provides very stable replicas and images of high contrast. Some other metals, such as tantalum (Ta) have been reported to provide better resolution on isolated macromolecular complexes and cellular structures. Our goal is to study the gain in detail with Ta and to evaluate if it provides enough detail and resolution to assist in the study of complex volumes of intact cellular structures obtained by methods that reach molecular resolution. To this purpose Pt and Ta replicas of cellular structures and viruses have been studied by transmission electron microscopy (TEM). Replicas of Ta show new details on the surface of two types of isolated viral particles such as 100 nm bunyaviruses and large, > 300 nm, vaccinia virus (VV). Inside cells, the structural pieces that build VV immature particles are visualized only in Ta replicas. Looking for smaller intracellular complexes, new details are also seen in nuclear pores from Ta replicas. Additional masses, most likely representing the cargo during transport, are distinguished in some of the pores. Visualization of proteins in plasma membranes strongly suggests that detail and resolution of Ta replicas are similar to those estimated for 3D maps currently obtained by electron tomography of viruses and cells.

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Structure of intracellular mature vaccinia virus observed by cryoelectron microscopy

Cited by 73 publications

References 19 publications

Supramolecular Architecture of Severe Acute Respiratory Syndrome Coronavirus Revealed by Electron Cryomicroscopy

Supramolecular Architecture of Severe Acute Respiratory Syndrome Coronavirus Revealed by Electron Cryomicroscopy

Deep-etch EM reveals that the early poxvirus envelope is a single membrane bilayer stabilized by a geodetic “honeycomb” surface coat

Studying cellular architecture in three dimensions with improved resolution: Ta replicas revisited

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