Placement of the Structural Proteins in Sindbis Virus

Zhang, Wei; Mukhopadhyay, Suchetana; Pletnev, Sergei; Baker, Timothy S.; Kühn, Richard; Rossmann, Michael G.

doi:10.1128/jvi.76.22.11645-11658.2002

Cited by 202 publications

(210 citation statements)

References 67 publications

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“…The estimated thickness of the outer layer of the AFV3 virion of 3.1 nm measured on the 2D average map corresponds closely with estimates for virions of other lipothrixviruses, namely, SIFV, AFV1, and AFV2, based on observed particle widths before and after removal of the outer layer (1,5,13). The value is less than the minimal observed widths of cellular or viral membranes (41) and raises the issue of the chemical composition of the outer layer. The fact that Triton X-100 can remove the outer envelope from the AFV3 virion (Fig.…”

Section: Discussionmentioning

confidence: 79%

Structure of the Acidianus Filamentous Virus 3 and Comparative Genomics of Related Archaeal Lipothrixviruses

Vestergaard

Aramayo

Basta

et al. 2008

J Virol

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Four novel filamentous viruses with double-stranded DNA genomes, namely, Acidianus filamentous virus 3 (AFV3), AFV6, AFV7, and AFV8, have been characterized from the hyperthermophilic archaeal genus Acidianus, and they are assigned to the Betalipothrixvirus genus of the family Lipothrixviridae. The structures of the approximately 2-m-long virions are similar, and one of them, AFV3, was studied in detail. It consists of a cylindrical envelope containing globular subunits arranged in a helical formation that is unique for any known double-stranded DNA virus. The envelope is 3.1 nm thick and encases an inner core with two parallel rows of protein subunits arranged like a zipper. Each end of the virion is tapered and carries three short filaments. Two major structural proteins were identified as being common to all betalipothrixviruses. The viral genomes were sequenced and analyzed, and they reveal a high level of conservation in both gene content and gene order over large regions, with this similarity extending partly to the earlier described betalipothrixvirus Sulfolobus islandicus filamentous virus. A few predicted gene products of each virus, in addition to the structural proteins, could be assigned specific functions, including a putative helicase involved in Holliday junction branch migration, a nuclease, a protein phosphatase, transcriptional regulators, and glycosyltransferases. The AFV7 genome appears to have undergone intergenomic recombination with a large section of an AFV2-like viral genome, apparently resulting in phenotypic changes, as revealed by the presence of AFV2-like termini in the AFV7 virions. Shared features of the genomes include (i) large inverted terminal repeats exhibiting conserved, regularly spaced direct repeats; (ii) a highly conserved operon encoding the two major structural proteins; (iii) multiple overlapping open reading frames, which may be indicative of gene recoding; (iv) putative 12-bp genetic elements; and (v) partial gene sequences corresponding closely to spacer sequences of chromosomal repeat clusters.

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Section: Discussionmentioning

confidence: 79%

Structure of the Acidianus Filamentous Virus 3 and Comparative Genomics of Related Archaeal Lipothrixviruses

Vestergaard

Aramayo

Basta

et al. 2008

J Virol

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“…33−36 Atomic structures of the CP alone have the Nterminus disordered, 37,38 and in the cryo electron microscopy structure of the virus, the N-terminus is positioned inward, making contacts with the viral RNA. 14,37,39 The C-terminal domain (residues 101−270) is a chymotrypsin-like domain that comprises a majority of the ordered nucleocapsid core seen in the alphavirus structure. 14,24 There are minimal CP−CP contacts in the C-terminal domain 14,40 suggesting electrostatic interactions between the basic charged N-terminal domain of CP and the acidic residues of the viral RNA drive nucleocapsid core formation.…”

Section: ■ Introductionmentioning

confidence: 99%

The Packaging of Different Cargo into Enveloped Viral Nanoparticles

Fan

Tsvetkova²,

Khuong³

et al. 2012

Mol. Pharmaceutics

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Viral nanoparticles used for biomedical applications must be able to discriminate between tumor or virus-infected host cells and healthy host cells. In addition, viral nanoparticles must have the flexibility to incorporate a wide range of cargo, from inorganic metals to mRNAs to small molecules. Alphaviruses are a family of enveloped viruses for which some species are intrinsically capable of systemic tumor targeting. Alphavirus virus-like particles, or viral nanoparticles, can be generated from in vitro self-assembled core-like particles using nonviral nucleic acid. In this work, we expand on the types of cargo that can be incorporated into alphavirus core-like particles and the molecular requirements for packaging this cargo. We demonstrate that different core-like particle templates can be further enveloped to form viral nanoparticles that are capable of cell entry. We propose that alphaviruses can be selectively modified to create viral nanoparticles for biomedical applications and basic research.

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“…[20][21][22] The outer protein shell contains 240 copies of glycoproteins, E1 and E2. 20,23,24 E1 causes cell fusion, whereas E2 is predominantly the protein responsible for cell membrane attachment. 19,[25][26][27][28][29] Importantly, the Sindbis E1 protein can fuse to cells independently of the receptor binding E2 protein.…”

Section: Introductionmentioning

confidence: 99%

Lentiviruses with trastuzumab bound to their envelopes can target and kill prostate cancer cells

Moussavi

et al. 2009

Cancer Gene Ther

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In this study, we took advantage of the overexpression of human epidermal growth factor receptor 2 (HER-2) in prostate cancers to design lentiviruses with modified envelope proteins that bind antibodies to specific cell-surface antigens. When bound to trastuzumab (Herceptin, Genentech, CA), lentiviruses were able to selectively infect androgen-sensitive LNCaP and castrationresistant C4-2 human prostate cancer cell lines, both of which express high levels of HER-2. To test for a therapeutic effect, we engineered our antibody-binding lentiviruses to express thymidine kinase, which can convert the non-toxic pro-drug ganciclovir (GCV) into a cytotoxic form. LNCaP and C4-2 cells infected by these viruses were sensitive to GCV killing. In vivo, C4-2 xenograft tumors treated either intratumorally or i.v. with trastuzumab-bound lentivirus expressed luciferase, although the latter route was less tumor specific. When a prostate-specific promoter for governing luciferase expression was combined with trastuzumab-mediated delivery, there was a further enrichment in targeting viral gene expression in prostate tumors. In conclusion, we found that although prostate cancers that express high levels of HER-2 are resistant to the killing effects of trastuzumab, they can be targeted for selective gene expression and destruction by viruses with envelope proteins engineered to bind this antibody.

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Placement of the Structural Proteins in Sindbis Virus

Cited by 202 publications

References 67 publications

Structure of the Acidianus Filamentous Virus 3 and Comparative Genomics of Related Archaeal Lipothrixviruses

Structure of the Acidianus Filamentous Virus 3 and Comparative Genomics of Related Archaeal Lipothrixviruses

The Packaging of Different Cargo into Enveloped Viral Nanoparticles

Lentiviruses with trastuzumab bound to their envelopes can target and kill prostate cancer cells

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