British Journal of Medicine and Medical Research · 2014 · 17 citations · 21 references
Life SciencesBiochemistryInfectious DiseasesInfectious Disease PathologyMolecular VirologyVirologyDisulfide Bond FormationEnzyme InhibitionHost Cell AttachmentViral EntryViral InfectionsVirus EntryDisulfide Bond Isomerase ActivityDisulfide Exchange ChemistryMembrane PenetrationProtein Disulfide IsomeraseRedox-active Small MoleculesThiol-disulfide ExchangeViral Envelope ProteinsVirus-host Membrane Interactions
It is known that the virulence of Ebola and other RNA enveloped viruses involves in the first step their attachment to host cell membranes.Following this initial step the virus enters the target cell cytoplasm by forming hydrophobic spikes that make holes in the membrane lipid bilayer.Formation of such spikes is catalyzed by the reduced form of viral protein disulfide isomerase (PDIred) thus initiating chain of disulfide exchange reactions.Consequently, hydrophobic protein epitopes become exposed, which in the absence of proper chaperones form hydrophobic 'spikes' capable of penetrating the host cell membranes.In this communication evidence is discussed showing that the chain of disulfide exchange events can be inhibited by a small redox moleculesodium selenite.It is suggested that this inexpensive and readily available food supplement can be an ultimate inhibitor of Ebola and other enveloped viral infections.
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Principles that Govern the Folding of Protein Chains
Christian B. Anfinsen · Science · 1973 · 7.1K citations
Hugues J.‐P. Ryser, Elinor M. Levy, Richard Mandel et al. · Proceedings of the National Academy of Sciences · 1994 · 275 citations