Viroporins: structure and biological functions

Nieva, José L.; Madan, Vanesa; Carrasco, Luís

doi:10.1038/nrmicro2820

Cited by 404 publications

(534 citation statements)

References 138 publications

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“…However, recent progress has extended to the structural characterization of hexameric two-TMD HCV p7 channels (OuYang et al, 2013). The number and orientation of TMDs has been proposed as a means of classifying viroporins, where class I/II refers to the number of TMDs and a/b subclasses nominate proteins with either lumenal or cytosolic N termini, respectively (Nieva et al, 2012). Whilst useful in many respects, viroporins predicted to possess three TMDs need to be included and this system does not account for the fact that structurally related viroporins rarely perform the same function within the infected cell.…”

Section: Viroporin Channel Functionsmentioning

confidence: 99%

Viroporins: structure, function and potential as antiviral targets

Scott

Griffin

2015

Journal of General Virology

120

146

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The channel-forming activity of a family of small, hydrophobic integral membrane proteins termed 'viroporins' is essential to the life cycles of an increasingly diverse range of RNA and DNA viruses, generating significant interest in targeting these proteins for antiviral development. Viroporins vary greatly in terms of their atomic structure and can perform multiple functions during the virus life cycle, including those distinct from their role as oligomeric membrane channels. Recent progress has seen an explosion in both the identification and understanding of many such proteins encoded by highly significant pathogens, yet the prototypic M2 proton channel of influenza A virus remains the only example of a viroporin with provenance as an antiviral drug target. This review attempts to summarize our current understanding of the channel-forming functions for key members of this growing family, including recent progress in structural studies and drug discovery research, as well as novel insights into the life cycles of many viruses revealed by a requirement for viroporin activity. Ultimately, given the successes of drugs targeting ion channels in other areas of medicine, unlocking the therapeutic potential of viroporins represents a valuable goal for many of the most significant viral challenges to human and animal health.

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Section: Viroporin Channel Functionsmentioning

confidence: 99%

Viroporins: structure, function and potential as antiviral targets

Scott

Griffin

2015

Journal of General Virology

120

146

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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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“…However, as viruses are bound to utilize the host cellular machinery to propagate, they are critically dependent on cellular factors that are up-or downregulated as needed. Examples are the down-regulation of membrane receptors [48][49][50][51][52][53] , the up-regulation of the lipid metabolism 54 , the use of the mRNA processing machinery 55 or the hijacking of components of the endosomal-sorting complex (ESCRT) required for virus export from infected cells [56][57][58][59][60][61][62][63] (see 2.4 for details). Moreover, as the life cycle of different viruses share common cellular factors and pathways, it is feasible that these could be used as targets for the design of broad-spectrum antivirals.…”

Section: One For Many: the Broad-spectrum Alternativementioning

confidence: 99%

Antiviral drug discovery: broad-spectrum drugs from nature

et al. 2015

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, but cannot be converted to PDF. You must view these files (e.g. movies) online.Scheme 1_(structures 1-5)_named.cdx Scheme 2_(structures 6-8)_named.cdx Scheme 3_(structure 9)_named.cdx Scheme 4_(structure 10)_named.cdx Scheme 5_ (structures 11-12) The development of drugs with broad-spectrum antiviral activities is a long pursued goal in drug discovery. It has been shown that blocking co-opted host-factors abrogates the replication of many viruses, yet the development of such host-targeting drugs has been met with skepticism mainly due to toxicity issues and poor translation to in vivo models. With the advent of new and more powerful screening assays and prediction tools, the idea of a drug that can efficiently treat a wide range of viral infections by blocking specific host functions has rebloomed. Here we critically review the state-of-the-art in broad-spectrum antiviral drug discovery. We discuss putative targets and treatment strategies, taking particular focus on natural products as promising starting points for antiviral lead development.

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Viroporins: structure and biological functions

Cited by 404 publications

References 138 publications

Viroporins: structure, function and potential as antiviral targets

Viroporins: structure, function and potential as antiviral targets

Potassium Ion Channels: Could They Have Evolved from Viruses?

Antiviral drug discovery: broad-spectrum drugs from nature

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