Modification of membrane permeability by animal viruses

Carrasco, Luís; Otero, Ma Jesús; Castrillo, José Luis

doi:10.1016/0163-7258(89)90096-x

Cited by 105 publications

(145 citation statements)

References 281 publications

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“…Recent reports suggest that this occurs. The K + channels in the chlorella viruses are just one example of a collection of viral proteins with channel function; these proteins have been given the name viroporins (Carrasco, 1995;Nieva et al, 2012;Schindler and Fischer, 2012). Since the seminal discovery of the M2 protein and its role as an H + channel in the influenza A virus (Pinto et al, 1992), there are an increasing number of reports that viruses from various families encode proteins with ion channel function.…”

Section: Additional Viruses Code For Ion Channel Proteinsmentioning

confidence: 99%

Potassium Ion Channels: Could They Have Evolved from Viruses?

et al. 2013

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Section: Additional Viruses Code For Ion Channel Proteinsmentioning

confidence: 99%

Potassium Ion Channels: Could They Have Evolved from Viruses?

et al. 2013

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“…An important membrane modification that can be observed in infected cells is the increase in membrane permeability, which affects both intracellular membranes and the plasma membrane (3)(4)(5). The gradual modification of membrane permeability starts with the release of calcium from intracellular stores, followed (or accompanied) by the disruption of ionic gradients over the plasma membrane.…”

mentioning

confidence: 99%

Mutational Analysis of Different Regions in the Coxsackievirus 2B Protein

Jong¹,

Melchers²,

Glaudemans³

et al. 2004

Journal of Biological Chemistry

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The coxsackievirus 2B protein is a small hydrophobic protein (99 amino acids) that increases host cell membrane permeability, possibly by forming homo-multimers that build membrane-integral pores. Previously, we defined the functional role of the two hydrophobic regions HR1 and HR2. Here, we investigated the importance of regions outside HR1 and HR2 for multimerization, increasing membrane permeability, subcellular localization, and virus replication through analysis of linker insertion and substitution mutants. From these studies, the following conclusions could be drawn. Enteroviruses (e.g. poliovirus, coxsackievirus, echovirus) belong to the family of Picornaviridae, a large family of nonenveloped, cytolytic viruses. The enterovirus genome consists of a 7.5-kb RNA molecule of positive polarity that is translated into one single 220-kDa polyprotein in a cap-independent manner.

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“…A widespread phenomenon during viral infection is the alteration of the permeability of the host plasma membrane (reviewed in Refs. [1][2][3]. Viruses can modify the membranes of their host cells in at least two ways: (i) by promoting membrane fusion between virus and cell and/or between cell and cell and (ii) by altering the permeability of the plasma membrane (reviewed in Ref.…”

mentioning

confidence: 99%

Modification of Late Membrane Permeability in Avian Reovirus-infected Cells

Bodelón

Labrada²,

Martı́nez-Costas

et al. 2002

Journal of Biological Chemistry

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Infection of chicken embryo fibroblasts by avian reovirus induces an increase in the permeability of the host plasma membrane at late, but not early, infection times. The absence of permeability changes at early infection times, as well as the dependence of late membrane modification on both viral protein synthesis and an active exocytic route, suggest that a virus-encoded membrane protein is required for avian reovirus to permeabilize cells. Further studies revealed that expression of nonstructural p10 protein in bacterial cells arrested cell growth and enhanced membrane permeability. Membrane leakiness was also observed following transient expression of p10 in BSC-40 monkey cells. Both its permeabilizing effect and the fact that p10 shares several structural and physical characteristics with other membrane-active viral proteins indicate that p10 is an avian reovirus viroporin. Furthermore, the fusogenic extracellular NH 2 -terminal domain of p10 appears to be dispensable for permeabilizing activity, because its deletion entirely abolished the fusogenic activity of p10, without affecting its ability to associate with cell membranes and to enhance membrane permeability. Similar properties have reported previously for immunodeficiency virus type I transmembrane glycoprotein gp41. Thus, like gp41, p10 appears to be a multifunctional protein that plays key roles in virus-host interaction.Cytolytic viruses induce profound injurious effects in susceptible host cells, resulting in morphological, structural, and biochemical changes and in cell degeneration. A widespread phenomenon during viral infection is the alteration of the permeability of the host plasma membrane (reviewed in Refs.

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Modification of membrane permeability by animal viruses

Cited by 105 publications

References 281 publications

Potassium Ion Channels: Could They Have Evolved from Viruses?

Potassium Ion Channels: Could They Have Evolved from Viruses?

Mutational Analysis of Different Regions in the Coxsackievirus 2B Protein

Modification of Late Membrane Permeability in Avian Reovirus-infected Cells

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