The Role of a 21-kDa Viral Membrane Protein in the Assembly of Vaccinia Virus from the Intermediate Compartment

Krijnse‐Locker, Jacomine; Schleich, Sibylle; Rodrı́guez, Dolores; Goud, Bruno; Snijder, Eric J.; Griffiths, Gareth

doi:10.1074/jbc.271.25.14950

Cited by 70 publications

(83 citation statements)

References 64 publications

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“…A fraction of intracellular mature VV (IMV) becomes further enveloped by a double membrane derived from the trans-Golgi network or early tubular endosomes (10,11) to form intracellular enveloped viruses. An important controversy has traditionally surrounded the origin and number of membranes that form VV crescents and IVs (12,13). The initial idea of a de novo synthesis of a single, primary VV membrane (13)(14)(15) has been recently disfavored.…”

Section: Accinia Virus (Vv) Is the Best-characterized Member Of Thementioning

confidence: 99%

Cryo-electron tomography of vaccinia virus

Cyrklaff

Risco²,

Fernández³

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

184

150

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The combination of cryo-microscopy and electron tomographic reconstruction has allowed us to determine the structure of one of the more complex viruses, intracellular mature vaccinia virus, at a resolution of 4 -6 nm. The tomographic reconstruction allows us to dissect the different structural components of the viral particle, avoiding projection artifacts derived from previous microscopic observations. A surface-rendering representation revealed brickshaped viral particles with slightly rounded edges and dimensions of Ϸ360 ؋ 270 ؋ 250 nm. The outer layer was consistent with a lipid membrane (5-6 nm thick), below which usually two lateral bodies were found, built up by a heterogeneous material without apparent ordering or repetitive features. The internal core presented an inner cavity with electron dense coils of presumptive DNA-protein complexes, together with areas of very low density. The core was surrounded by two layers comprising an overall thickness of Ϸ18 -19 nm; the inner layer was consistent with a lipid membrane. The outer layer was discontinuous, formed by a periodic palisade built by the side interaction of T-shaped protein spikes that were anchored in the lower membrane and were arranged into small hexagonal crystallites. It was possible to detect a few pore-like structures that communicated the inner side of the core with the region outside the layer built by the T-shaped spike palisade.cryo-EM ͉ virus structure ͉ 3D reconstruction

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Section: Accinia Virus (Vv) Is the Best-characterized Member Of Thementioning

confidence: 99%

Cryo-electron tomography of vaccinia virus

Cyrklaff

Risco²,

Fernández³

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

184

150

View full text Add to dashboard Cite

show abstract

“…1B) (23,31,34). The processed A17 protein spans the membrane twice, and both ends of the protein are oriented toward the cytoplasm in the infected cells (35,36). After being packaged into MV particles, the N terminus of A17 is exposed on the surface of the virions, whereas the C terminus appears embedded within the viral membranes (36,37).…”

mentioning

confidence: 99%

“…4, B-D). The F1-binding site presents as a twisted bended motif due to the presence of Pro 35 , whereas the F2-binding site has a zigzag backbone conformation; both the F1-and F2-binding sites are suitable for accommodating the ␣-helical motif. To reconstruct the A27-A17 protein complex, we conducted a molecular docking analysis of the ␣-helical A27 segment (Phe 80 -Asp…”

mentioning

confidence: 99%

Vaccinia Viral Protein A27 Is Anchored to the Viral Membrane via a Cooperative Interaction with Viral Membrane Protein A17

Wang

Hsiao

Wong

et al. 2014

Journal of Biological Chemistry

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Background: Vaccinia viral protein A27 associates with viral membrane protein A17 for anchoring to the viral membrane. Results: A27 specifically interacts with two binding regions within the N-terminal domain of A17. Conclusion: The A27-A17 interaction is mediated through a specific and cooperative binding mechanism. Significance: As demonstrated, the F1 and F2 bindings are critical for A27 anchoring to the viral membrane and virion assembly.

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“…Immunoelectron microscopy of infected cells indicated the presence of viral transmembrane proteins in smooth tubules that react with antibodies to endoplasmic reticulum (ER) and ER-Golgi intermediate compartment (ERGIC) markers and the occurrence of such tubules near and possibly connected to viral crescent membranes (4,7,8,(10)(11)(12). However, the presence of viral proteins in the secretory pathway could represent escape from the correct route to the viral membrane.…”

mentioning

confidence: 99%

Existence of an operative pathway from the endoplasmic reticulum to the immature poxvirus membrane

Husain

Weisberg

Moss

2006

Proc. Natl. Acad. Sci. U.S.A.

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In thin sections of cells infected with vaccinia virus or other poxviruses, the viral membrane is first discerned as a crescent or circle lacking obvious continuity with a cellular organelle, presenting an appearance of de novo membrane biogenesis. This notion, which many consider heretical, is nevertheless consistent with the absence of a signature of endoplasmic reticulum (ER) trafficking, such as signal peptide cleavage or glycosylation, in any of the numerous viral membrane proteins. The purpose of this study was to determine whether an operative pathway exists between the ER and the immature virion membrane. We showed that the highly conserved A9 viral membrane protein was inserted into the ER of uninfected cells with the same topology as in viral membranes. Next, we found that replacement of the nonessential cytoplasmic tail of A9 with one containing COPII-binding sites reduced incorporation of the modified A9 into viral membranes and led to its accumulation in the Golgi apparatus, implying that A9 was inserted into the ER and then diverted from its natural path. Most importantly, we demonstrated cleavage of a heterologous signal peptide fused to the N-terminal region of A9 and localized the truncated protein in immature and mature virions. Additionally, immunoelectron micrographs showed A9 in tubules containing protein disulfide isomerase, an ER lumenal protein, near immature viral membranes. The present data provide strong evidence for an operative pathway from ER domains within the virus factory to the viral membrane. membrane protein trafficking ͉ vaccinia virus ͉ virus assembly

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The Role of a 21-kDa Viral Membrane Protein in the Assembly of Vaccinia Virus from the Intermediate Compartment

Abstract: Taken together, these data provide the first molecular evidence in support of our assembly model; they show that an essential membrane protein of the IMV inserts into the rough endoplasmic reticulum, but gets efficiently targeted to the IC and membranes of the viral factory.

Cited by 70 publications

References 64 publications

Cryo-electron tomography of vaccinia virus

Cryo-electron tomography of vaccinia virus

Vaccinia Viral Protein A27 Is Anchored to the Viral Membrane via a Cooperative Interaction with Viral Membrane Protein A17

Existence of an operative pathway from the endoplasmic reticulum to the immature poxvirus membrane

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