Characterization of revertants of a Sindbis virus 6K gene mutant that affects proteolytic processing and virus assembly

Ivanova, Lidia; Le, Lam; Schlesinger, Milton J.

doi:10.1016/0168-1702(95)00083-6

Cited by 18 publications

(19 citation statements)

References 14 publications

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“…Given that E1 is not produced during frameshift events and that capsid is soluble in the cytoplasm, TF may require interaction with E2. Indeed, genetic evidence suggests an interaction between a domain of 6K shared with TF and the E2 protein (38,39). Our data also suggest that the length of the TF protein is important, as even a deletion of the C-terminal 7 residues of TF reduced multiplication to a level similar to that in the ⌬TF virus.…”

Section: Discussionsupporting

confidence: 59%

Functional Characterization of the Alphavirus TF Protein

Snyder

Kulcsar

Schultz

et al. 2013

J Virol

128

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Here, we validate the findings of Firth and colleagues with respect to the production of the TF protein and begin to characterize the function of TF. Using a mass spectrometry-based approach, we identified TF in purified preparations of both Sindbis and Chikungunya virus particles. We next constructed a panel of Sindbis virus mutants with mutations which alter the production, size, or sequence of TF. We demonstrate that TF is not absolutely required in culture, although disrupting TF production leads to a decrease in virus particle release in both mammalian and insect cells. In a mouse neuropathogenesis model, mortality was <15% in animals infected with the TF mutants, whereas mortality was 95% in animals infected with the wild-type virus. Using a variety of additional assays, we demonstrate that TF retains ion-channel activity analogous to that of 6K and that lack of production of TF does not affect genome replication, particle infectivity, or envelope protein transit to the cell surface. The TF protein therefore represents a previously uncharacterized factor important for alphavirus assembly.

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Section: Discussionsupporting

confidence: 59%

Functional Characterization of the Alphavirus TF Protein

Snyder

Kulcsar

Schultz

et al. 2013

J Virol

128

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“…Our evidence that 6K has a single transmembrane domain is in contrast with earlier results suggesting that 6K crosses the membrane twice, with both termini exposed to the lumen of the ER (1,38). However, these data do not exclude the possibility that the C-terminus of 6K is only transiently located in the ER lumen.…”

Section: Fig 6 Bfv 6k Ion Channelscontrasting

confidence: 56%

“…No gross structural abnormalities have been noted in 6K-deleted virions although, in SFV, the mutant virions are more heat-labile (6). Budding defects caused by point mutations in 6K can be rescued by a second-site mutation in glycoprotein E2 (38), hinting at an interrelationship between 6K, the E2 protein, and lipid (10). Budding defects have additionally been noted when SINV 6K cysteine residues that normally acquire a palmitoyl group are mutated (8).…”

Section: Fig 6 Bfv 6k Ion Channelsmentioning

confidence: 85%

Alphavirus 6K Proteins Form Ion Channels

Melton

Ewart

Weir

et al. 2002

Journal of Biological Chemistry

112

101

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Ross River virus and Barmah Forest virus are Australian arboviruses of the Alphavirus genus. Features of alphavirus infection include an increased permeability of cells to monovalent cations followed by virion budding. Virally encoded ion channels are thought to have a role in these processes. In this paper, the 6K proteins of Ross River virus and Barmah Forest virus are shown to form cation-selective ion channels in planar lipid bilayers. Using a novel purification method, bacterially expressed 6K proteins were inserted into bilayers with a defined orientation (i.e. N-terminal cis, C-terminal trans). Channel activity was reversibly inhibited by antibodies to the N and C termini of 6K protein added to the cis and trans baths, respectively. Channel conductances varied from 40 -800 picosiemens, suggesting that the protein is able to form channels with a range of possible oligomerization states.

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“…Rubella virus (family Togaviridae) capsid protein and the two envelope glycoproteins E1 and E2 form VLPs by a budding mechanism. The E2 transmembrane and cytoplasmic domain contains retention signals which are required for interaction with the capsid and VLP secretion (Ivanova et al, 1995).…”

Section: Cell Membranesmentioning

confidence: 99%