Modification of Membrane Permeability by Animal Viruses

Carrasco, Luís; Pérez, Luis; Irurzun, Alicia; Lama, Juan; Martı́nez-Abarca, Francisco; Rodrı́guez, Pedro L.; Guinea, Rosario; Castrillo, José Luis; Ángel, Miguel; José, Ma Isabel De

doi:10.1007/978-1-4615-2928-6_20

Cited by 44 publications

(51 citation statements)

References 96 publications

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“…Some antiviral inhibitory effects were already explained by the entry of hydrophobic inhibitory molecules in the hydrophobic binding cavities on the viral surface (Cox et al, 1996;O'Connell, Albin, Blum, Grint, & Schwartz, 1995). Although enteroviruses are not endowed with any membranes, they interact with cellular membranes and provoke changes in their organization (Carrasco, 1995;Sandoval & Carrasco, 1997).…”

Section: Introductionmentioning

confidence: 98%

The effect of bovine whey proteins on the ability of poliovirus and Coxsackie virus to infect Vero cell cultures

Sitohy

Dalgalarrondo

Nowoczin

et al. 2008

International Dairy Journal

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Section: Introductionmentioning

confidence: 98%

The effect of bovine whey proteins on the ability of poliovirus and Coxsackie virus to infect Vero cell cultures

Sitohy

Dalgalarrondo

Nowoczin

et al. 2008

International Dairy Journal

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“…1,2,8,9 To date, no functional homolog of viral origin similar to these ancient weapons has been discovered, even though enhanced membrane permeability is typically observed during infection of susceptible cells by most animal viruses. 10 Membrane permeabilization, together with morphological alterations induced by virus replication such as nuclear modifications, disruption of the cytoskeletal network, [11][12][13] and the appearance of cytoplasmic membrane vesicles have been referred to collectively as the cytopathic effect. 14,15 In the case of naked viruses, intracellular accumulation of viral particles and/or massive expression of viral products have often been causally linked to non-specific membrane damage processes that are postulated to enhance permeability, cell lysis and ultimately release of new progeny.…”

Section: Introductionmentioning

confidence: 99%

Plasma Membrane-porating Domain in Poliovirus 2B Protein. A Short Peptide Mimics Viroporin Activity

Madan

Sánchez-Martínez

Vedovato

et al. 2007

Journal of Molecular Biology

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Picornavirus 2B, a non-structural protein required for effective viral replication, has been implicated in cell membrane permeabilization during the late phases of infection. Here, we have approached the molecular mechanism of this process by assessing the pore-forming activity of an overlapping peptide library that spanned the complete 2B sequence. At non-cytopathic concentrations, only the P3 peptide, spanning 2B residues 35-55, effectively assembled hydrophilic pores that allowed diffusion of low molecular mass solutes across the cell plasma membrane (IC(50) approximately 4x10(-7) M) and boundary liposome bilayers (starting at peptide to lipid molar ratios>1:10(4)). Circular dichroism data were consistent with its capacity to fold as a helix in a membrane-like environment. Furthermore, addition of this peptide to a sealed plasma-membrane model, consisting of retinal rod outer segments patch-clamped in a whole-cell configuration, induced ion channel activity within seconds at concentrations as low as 10(-8) M. Thus, we have established a "one-helix" 2B version that possesses the intrinsic pore-forming activity required to directly and effectively permeabilize the cell plasma membrane. We conclude that 2B viroporin can be classified as a genuine pore-forming toxin of viral origin, which is produced intracellularly at certain times post infection.

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“…Therefore, animal viruses dissipate the ionic gradients during entry. The physiological significance of this behaviour may be to couple the proton motive force with virus entry into the cytoplasm [19].…”

Section: R Guinea L Carrascolfebsmentioning

confidence: 99%

Concanamycin A blocks influenza virus entry into cells under acidic conditions

Guinea

Carrasco

1994

FEBS Letters

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The selective inhibitor of the vacuolar proton-ATPase, concanamycin A, powerfully blocks influenza virus entry into cells, if present during the initial times of virus infection. Attachment of virus particles to cells is not prevented by concanamycin A, rather the exit of influenza virus from endosomes is the step blocked by this macrolide antibiotic. Inhibition of influenza virus entry into cells by concanamycin A or by nigericin takes place under acidic conditions. Moreover, if the pH gradient is abolished by pre-incubation of cells in acidic pH, influenza virus entry does not occur even in the absence of any inhibitors. These results indicate that acidic conditions per se are not sufficient to promote virus entry into cells; rather this step of virus infection requires a pH gradient.

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Modification of Membrane Permeability by Animal Viruses

Cited by 44 publications

References 96 publications

The effect of bovine whey proteins on the ability of poliovirus and Coxsackie virus to infect Vero cell cultures

The effect of bovine whey proteins on the ability of poliovirus and Coxsackie virus to infect Vero cell cultures

Plasma Membrane-porating Domain in Poliovirus 2B Protein. A Short Peptide Mimics Viroporin Activity

Concanamycin A blocks influenza virus entry into cells under acidic conditions

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