Viral Proteins that Enhance Membrane Permeability

González, María Eugenia Pérez; Carrasco, Luís

doi:10.1007/0-387-28146-0_6

Cited by 3 publications

(6 citation statements)

References 64 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…To date, the majority of efforts to develop specific anti-Vpu drugs have concentrated on the ability of viroporins to disturb ionic currents in membranes. This strategy has led to the search for inhibitors of other viroporins [ 105 ]. The first approaches to search for Vpu inhibitors utilized the measurement of ionic currents in artificial planar lipid bilayers [ 106 ], a methodology that led to the discovery of 5-(N,N-Hexamethylene) amiloride (HMA) as the first Vpu inhibitor [ 107 ].…”

Section: Vpu Viroporin As a Therapeutic Targetmentioning

confidence: 99%

Vpu Protein: The Viroporin Encoded by HIV-1

González

2015

Viruses

View full text Add to dashboard Cite

Viral protein U (Vpu) is a lentiviral viroporin encoded by human immunodeficiency virus type 1 (HIV-1) and some simian immunodeficiency virus (SIV) strains. This small protein of 81 amino acids contains a single transmembrane domain that allows for supramolecular organization via homoligomerization or interaction with other proteins. The topology and trafficking of Vpu through subcellular compartments result in pleiotropic effects in host cells. Notwithstanding the high variability of its amino acid sequence, the functionality of Vpu is well conserved in pandemic virus isolates. This review outlines our current knowledge on the interactions of Vpu with the host cell. The regulation of cellular physiology by Vpu and the validity of this viroporin as a therapeutic target are also discussed.

show abstract

Section: Vpu Viroporin As a Therapeutic Targetmentioning

confidence: 99%

Vpu Protein: The Viroporin Encoded by HIV-1

González

2015

Viruses

View full text Add to dashboard Cite

show abstract

“…However, there is a class of membrane-embedded proteins termed VPs that are essential for virulence and infectivity (444)(445)(446) and have proven to be a valuable but yet elusive targets for therapies. VPs are small transmembrane proteins (60-120 amino acids) that oligomerize into ion channels capable of permeabilizing cell membranes (447). They are classified into class I for single pass TMs and class II for helix-turn-helix hairpin motifs (445,447).…”

Section: How Small Viral Transmembrane Proteins Could Be a Linchpin Of Viral Infection?mentioning

confidence: 99%

“…VPs are small transmembrane proteins (60-120 amino acids) that oligomerize into ion channels capable of permeabilizing cell membranes (447). They are classified into class I for single pass TMs and class II for helix-turn-helix hairpin motifs (445,447). Among the most studied VPs are the M2 proteins from Influenza A (IA) (448)(449)(450)(451)(452)(453)(454)(455) and Influenza B (456,457), VpU from HIV (458-467), the Envelope protein from Coronaviridae (468)(469)(470)(471), and the p7 protein from Hepatitis C virus (472-476) (Fig.…”

Section: How Small Viral Transmembrane Proteins Could Be a Linchpin Of Viral Infection?mentioning

confidence: 99%

Highlighting membrane protein structure and function: A celebration of the Protein Data Bank

Egea

Vecchio

et al. 2021

Journal of Biological Chemistry

View full text Add to dashboard Cite

“…Once a candidate viroporin is identified, a wide variety of functional assays can be used to test for viroporin activity. The most commonly used assays measure the viroporin’s ability to induce PM permeability upon recombinant expression in either E. coli or mammalian cells (reviewed in 2, 21).…”

Section: Identification and Functional Characterization Of Candidate mentioning

confidence: 99%

“…Mammalian cell permeability assays are conducted in a similar fashion, such that virus infection or viroporin expression increases the cell’s permeability to small molecules. For mammalian cells, use of translation inhibitors (e.g., hygromycin B) and 35 S-methionine labeling of protein synthesis or fluorescent molecules (e.g., propidium iodide) are the most commonly employed techniques (21).…”

Section: Identification and Functional Characterization Of Candidate mentioning

confidence: 99%

Pathophysiological Consequences of Calcium-Conducting Viroporins

2015

View full text Add to dashboard Cite

Eukaryotic cells have evolved a myriad of ion channels, transporters, and pumps to maintain and regulate transmembrane ion gradients. As intracellular parasites, viruses also have evolved ion channel proteins, called viroporins, which disrupt normal ionic homeostasis to promote viral replication and pathogenesis. The first viral ion channel (influenza M2 protein) was confirmed only 23 years ago, and since then studies on M2 and many other viroporins have shown they serve critical functions in virus entry, replication, morphogenesis, and immune evasion. As new candidate viroporins and viroporin-mediated functions are being discovered, we review the experimental criteria for viroporin identification and characterization to facilitate consistency within this field of research. Then we review recent studies on how the few Ca(2+)-conducting viroporins exploit host signaling pathways, including store-operated Ca(2+) entry, autophagy, and inflammasome activation. These viroporin-induced aberrant Ca(2+) signals cause pathophysiological changes resulting in diarrhea, vomiting, and proinflammatory diseases, making both the viroporin and host Ca(2+) signaling pathways potential therapeutic targets for antiviral drugs.

show abstract

Viral Proteins that Enhance Membrane Permeability

Cited by 3 publications

References 64 publications

Vpu Protein: The Viroporin Encoded by HIV-1

Vpu Protein: The Viroporin Encoded by HIV-1

Highlighting membrane protein structure and function: A celebration of the Protein Data Bank

Pathophysiological Consequences of Calcium-Conducting Viroporins

Contact Info

Product

Resources

About