Viral Translation Inhibitors

Carrasco, Luís; Vázquez, David

doi:10.1007/978-3-642-68946-8_18

Cited by 5 publications

(4 citation statements)

References 92 publications

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“…Several reports in the literature indicate that HyB enters the cell and inhibits protein synthesis only when membrane permeability is modified (2,4,5,7,13). According to this hypothesis, HCMV infection seems to induce an altered membrane permeability both immediately after virus adsorption and in concomitance with viral release.…”

Section: Discussionmentioning

confidence: 98%

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Changes in membrane permeability in cells infected by human cytomegalovirus

Rugolo

Baldassarri

Landini

1986

Archives of Virology

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To analyze whether human cytomegalovirus could induce changes in membrane permeability we studied both Hygromycin B (HyB) inhibition of protein synthesis and glycine and choline uptake during viral replication. A higher sensitivity to HyB was observed both immediately after virus adsorption and in concomitance with the release of viral progeny. HyB sensitivity immediately after virus adsorption was not associated with changes in membrane permeability to glycine and choline while 60 hours p.i. a remarkable increase in choline uptake was detected.

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Section: Discussionmentioning

confidence: 98%

“…This compound has been suggested to enter the ceil and block protein synthesis when membrane permeability becomes modified (5). One was based on the use of Hygromyein B (IIyB), a translation inhibitor which does not block protein synthesis in normal mammalian cells because it fails to permeate the membrane barrier.…”

Section: Introductionmentioning

confidence: 99%

Changes in membrane permeability in cells infected by human cytomegalovirus

Rugolo

Baldassarri

Landini

1986

Archives of Virology

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“…Different tests have been used to analyze alterations of membrane permeability (10). To measure the efflux of compounds, the release of radioactivity from uridine-loaded cells was tested, while the increased entry of compounds was performed with the hygromycin B test (12,17). Bacteria were loaded with [ 3 H]uridine, and the release of radioactivity was analyzed after induction of gp41 and its fragments (Fig.…”

Section: Cloning and Expression Of Hiv-1 Gp41 And Its Fragments In Ementioning

confidence: 99%

“…A significant but small efflux was also observed with fragment B. A number of translation inhibitors do not block protein synthesis in intact cells because of the permeability barrier due to the cell membrane (12). These compounds readily enter into virus-infected cells or in cells treated with membrane-active compounds (1,8,17).…”

Section: Cloning and Expression Of Hiv-1 Gp41 And Its Fragments In Ementioning

confidence: 99%

Membrane permeabilization by different regions of the human immunodeficiency virus type 1 transmembrane glycoprotein gp41

Arroyo

Boceta

González

et al. 1995

J Virol

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The transmembrane glycoprotein (gp41) of human immunodeficiency virus type 1 (HIV-1) has been implicated in the cytopathology observed during HIV infection. The first amino acids located at the amino terminus are involved in membrane fusion and syncytium formation, while sequences located at the carboxy terminus have been predicted to interact with membranes and modify membrane permeability. The HIV-1 gp41 gene has been cloned and expressed in Escherichia coli cells by using pET vectors to analyze changes in membrane permeability produced by this protein. This system is well suited for expressing toxic genes in an inducible manner and for analyzing the function of proteins that modify membrane permeability. gp41 enhances the permeability of the bacterial membrane to hygromycin B despite the low level of expression of this protein. To localize the regions of gp41 responsible for these effects, a number of fragments spanning different portions of gp41 were inducibly expressed in E. coli. Two regions of gp41 were shown to increase membrane permeability: one located at the carboxy terminus, where two highly amphipathic helices have been predicted, and another one corresponding to the membrane-spanning domain. Expression of the central region of gp41 comprising this domain was highly lytic for E. coli cells and increased membrane permeability to a number of compounds. These findings are discussed in the light of HIV-induced cytopathology and gp41 structure.

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Influenza virus M2 protein modifies membrane permeability in E. coli cells

Guinea

Carrasco

1994

FEBS Letters

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The M2 protein of influenza virus is an integral membrane protein with ion channel activity. This protein has been expressed in E. coli cells in an inducible manner. Expression of the M2 protein causes rapid lysis of BL2l@E3) pLysS E. coli cells upon induction with IFTG. M2 protein increases membrane permeability to a number of hydrophylic molecules, such as ONPG, uridine or impermeant translation inhibitors. The behaviour of M2 in bacteria resembles that of other viral proteins, such as poliovirus 3A and Semliki Forest virus 6K.

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Viral Translation Inhibitors

Cited by 5 publications

References 92 publications

Changes in membrane permeability in cells infected by human cytomegalovirus

Changes in membrane permeability in cells infected by human cytomegalovirus

Membrane permeabilization by different regions of the human immunodeficiency virus type 1 transmembrane glycoprotein gp41

Influenza virus M2 protein modifies membrane permeability in E. coli cells

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