2020
DOI: 10.1016/j.bbamem.2019.183149
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Peptides derived from the C-terminal domain of HIV-1 Viral Protein R in lipid bilayers: Structure, membrane positioning and gene delivery

Abstract: Viral protein R (Vpr) is a small accessory protein of 96 amino acids that is present in Human and simian immunodeficiency viruses. Among the very different properties that Vpr possesses we can find cell penetrating capabilities. Based on this and on its capacity to interact with nucleic acids we previously investigated the DNA transfection properties of Vpr and subfragments thereof. We found that fragments of the C-terminal helical domain of Vpr are able to deliver efficiently plasmid DNA into different cell l… Show more

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Cited by 16 publications
(9 citation statements)
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“…Altogether, these studies suggested that viral glycoproteins might target raft domains within the mammalian plasma membrane (Figure 3b). In addition, negatively charged phospholipids, such as PS, can also affect the adsorption and the membrane location of fusion peptides, as shown in a recent study involving POPC/POPS vesicles and peptides derived from the C-terminal domain of HIV-1 viral protein R [114]. Glycoproteins of other enveloped viruses such as influenza or SARS-CoV viruses were also shown to have a strong association with raft-like lipid domains [54,115].…”
Section: Protein-lipid Interactionsmentioning
confidence: 95%
“…Altogether, these studies suggested that viral glycoproteins might target raft domains within the mammalian plasma membrane (Figure 3b). In addition, negatively charged phospholipids, such as PS, can also affect the adsorption and the membrane location of fusion peptides, as shown in a recent study involving POPC/POPS vesicles and peptides derived from the C-terminal domain of HIV-1 viral protein R [114]. Glycoproteins of other enveloped viruses such as influenza or SARS-CoV viruses were also shown to have a strong association with raft-like lipid domains [54,115].…”
Section: Protein-lipid Interactionsmentioning
confidence: 95%
“…5c). It has been shown that mHTT has high affinity for bioengineered lipid membranes and that insertion of these proteins into these membranes triggers their aggregation 47 . Our analysis also revealed that the largest HTTEx1Q72-mCherry puncta (volume > 5 µm 3 ) were nearly all (90-100%) localized at the myotube surface at DCC 7-21 (Fig.…”
Section: Modulating Neuronal Activity Alters Nm Transmission Of Mhttex1mentioning
confidence: 99%
“…The interactions of the peptides with the bilayer interface eventually result in pore-formation [191] and membrane lysis [192], thereby modulating nucleic acid delivery. Inspired by the ability to enhance the efficiency of several gene delivery systems, researchers in the past extensively used LAH4 peptides as targeting moiety [187,[193][194][195][196][197][198]. By now, there is a growing number of peptidic, as well as polymeric and lipidic carriers that utilize other histidine-rich moieties, such as O 10 H 6 [199], MS(O 10 H 6 ) [200,201], histidine-rich Tat peptide [202][203][204], or His6 RPCs [205,206] to develop new promising gene delivery strategies.…”
Section: Histidine-rich Peptidesmentioning
confidence: 99%