Influenza virus M2 protein modifies membrane permeability in <i>E. coli</i> cells

Guinea, Rosario; Carrasco, Luís

doi:10.1016/0014-5793(94)80564-4

Cited by 53 publications

(52 citation statements)

References 32 publications

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“…Their functions are related to both the modification of cell permeability to ions and membrane destabilization. The use of viroporins to promote progeny release is common to several families of viruses, such as picornavirus (38,44), retrovirus (45), and orthomyxoviruses (46). In this context, our results suggest that, as a consequence of the selective pressure exerted in human xenografted tumors in vivo, adenovirus has evolved to incorporate an alternative and more efficient mechanism of release, which it lacks in its native form (where it uses ADP as the main mechanism), but that other animal viruses have previously selected.…”

Section: Discussionmentioning

confidence: 99%

Bioselection of a Gain of Function Mutation that Enhances Adenovirus 5 Release and Improves Its Antitumoral Potency

et al. 2008

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Genetic bioselection of a mutagenized Ad5wt stock in human tumor xenografts led us to isolate AdT1, a mutant displaying a large-plaque phenotype in vitro and an enhanced systemic antitumor activity in vivo. AdT1 phenotype correlates with an increased progeny release without affecting total viral yield in different human tumors and cancer-associated fibroblasts. An approach combining hybrid Ad5/AdT1 recombinants and sequencing identified a truncating insertion in the endoplasmic reticulum retention domain of the E3/19K protein (445A mutation) which relocates the protein to the plasma membrane and is responsible for AdT1's enhanced release.

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Section: Discussionmentioning

confidence: 99%

Bioselection of a Gain of Function Mutation that Enhances Adenovirus 5 Release and Improves Its Antitumoral Potency

et al. 2008

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“…6,19 M2 proton channel activity is known to be cytotoxic in heterologous expression systems, such as E. coli, 20,21 with especially severe effects seen in insect cells and S. cerevisiae, with no overt toxicity observed in vertebrate cells. 21,22 …”

Section: © 2 0 0 7 L a N D E S B I O S C I E N C E D O N O T D I S mentioning

confidence: 99%

Toxicity of Influenza A Virus Matrix Protein 2 for Mammalian Cells is Associated with its Intrinsic Proton-Channeling Activity

Ilyinskii¹,

Gabai²,

Sunyaev³

et al. 2007

Cell Cycle

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“…The ONPG bacterial permeabilization assay was performed as previously described (26,34). pET-6HIS clones were transformed into BL21(DE3) cells (Novagen) and grown overnight at 37°C in LB containing 50 g of kanamycin per ml.…”

Section: Reagentsmentioning

confidence: 99%

“…In order to assay the function of VP5* mutants, we used a bacterial membrane permeability assay previously used to study fusion and channel-forming proteins (26,32). VP5*, VP5* truncations as well as VP8*, VP4, and the empty pET-6HIS plasmid were assayed for their ability to permeabilize E. coli following IPTG induction.…”

Section: Vp5* Permeabilizes Bl21(de3) Cellsmentioning

confidence: 99%

“…In order to investigate the role of the VP5*-HD in membrane permeability, we generated a series of VP5* mutants and evaluated their function by using a bacterial permeability assay originally developed to investigate the function of viral fusion and pore-forming proteins (26,32). Our findings demonstrate that VP5* proteins which permeabilize liposomes and cells contain the HD (residues 385 to 404) and that permeability is abolished by C-terminal truncations which remove a conserved GGA motif (residues 399 to 401) or by site-directed mutagenesis of the HD.…”

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Selective Membrane Permeabilization by the Rotavirus VP5* Protein Is Abrogated by Mutations in an Internal Hydrophobic Domain

Dowling

Denisova²,

LaMonica

et al. 2000

J Virol

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Rotavirus infectivity is dependent on the proteolytic cleavage of the VP4 spike protein into VP8* and VP5* proteins. Proteolytically activated virus, as well as expressed VP5*, permeabilizes membranes, suggesting that cleavage exposes a membrane-interactive domain of VP5* which effects rapid viral entry. The VP5* protein contains a single long hydrophobic domain (VP5*-HD, residues 385 to 404) at an internal site. In order to address the role of the VP5*-HD in permeabilizing cellular membranes, we analyzed the entry of o-nitrophenyl-␤-D-galactopyranoside (ONPG) into cells induced to express VP5* or mutated VP5* polypeptides. Following IPTG (isopropyl-␤-D-thiogalactopyranoside) induction, VP5* and VP5* truncations containing the VP5*-HD permeabilized cells to the entry and cleavage of ONPG, while VP8* and control proteins had no effect on cellular permeability. Expression of VP5* deletions containing residues 265 to 474 or 265 to 404 permeabilized cells; however, C-terminal truncations which remove the conserved GGA (residues 399 to 401) within the HD abolished membrane permeability. Site-directed mutagenesis of the VP5-HD further demonstrated a requirement for residues within the HD for VP5*-induced membrane permeability. Functional analysis of mutant VP5*s indicate that conserved glycines within the HD are required and suggest that a random coiled structure rather than the strictly hydrophobic character of the domain is required for permeability. Expressed VP5* did not alter bacterial growth kinetics or lyse bacteria following induction. Instead, VP5*-mediated size-selective membrane permeability, releasing 376-Da carboxyfluorescein but not 4-kDa fluorescein isothiocyanate-dextran from preloaded liposomes. These findings suggest that the fundamental role for VP5* in the rotavirus entry process may be to expose triple-layered particles to low [Ca] i , which uncoats the virus, rather than to effect the detergent-like lysis of early endosomal membranes.

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

Cited by 53 publications

References 32 publications

Bioselection of a Gain of Function Mutation that Enhances Adenovirus 5 Release and Improves Its Antitumoral Potency

Bioselection of a Gain of Function Mutation that Enhances Adenovirus 5 Release and Improves Its Antitumoral Potency

Toxicity of Influenza A Virus Matrix Protein 2 for Mammalian Cells is Associated with its Intrinsic Proton-Channeling Activity

Selective Membrane Permeabilization by the Rotavirus VP5* Protein Is Abrogated by Mutations in an Internal Hydrophobic Domain

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