Effect of Phospholipid Composition on an Amphipathic Peptide-Mediated Pore Formation in Bilayer Vesicles

Nicol, François; Nir, Shlomo; Szoka, Francis C.

doi:10.1016/s0006-3495(00)76639-2

Cited by 59 publications

(50 citation statements)

References 68 publications

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“…Recent nuclear magnetic spectroscopy resonance data have added support to this type of HIV c -membrane interaction (59). This surface state has been shown to be more energetically favored in lipids containing less ordered acyl chains that better accommodate the head group displacement because of peptide insertion (36). The local increase of ordered acyl chains in SPM-rich gel-phase domains might favor the inserted state of the peptide, which would increase the probability of subsequent pore formation.…”

Section: Discussionmentioning

confidence: 99%

“…In most of the cases, the surface aggregation of the peptides is not irreversible and depends on K s ϭ C/D, in which C and D denote on and off rate constants of surface aggregation (33,34). In later studies on the peptide GALA (35,36), the importance of peptide translocation was emphasized and it was suggested that the surface-associated GALA monomers or aggregates are stabilized in bilayers composed of phospholipids containing a cis unsaturation per acyl chain, which reduces transbilayer insertion.…”

Section: Analysis Of Leakage Viamentioning

confidence: 99%

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Sphingomyelin and Cholesterol Promote HIV-1 gp41 Pretransmembrane Sequence Surface Aggregation and Membrane Restructuring

Sáez‐Cirión

Nir

Lorizate

et al. 2002

Journal of Biological Chemistry

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122

136

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The interfacial sequence DKWASLWNWFNITNWL-WYIK, preceding the transmembrane anchor of gp41 glycoprotein subunit, has been shown to be essential for fusion activity and incorporation into virions. HIV c , a peptide representing this region, formed lytic pores in liposomes composed of the main lipids occurring in the human immunodeficiency virus, type 1 (HIV-1), envelope, i.e. 1-palmitoyl-2-oleoylphosphatidylcholine (POPC):sphingomyelin (SPM):cholesterol (Chol) (1:1:1 mole ratio), at low (>1:10,000) peptide-to-lipid mole ratio, and promoted the mixing of vesicular lipids at >1: 1000 peptide-to-lipid mole ratios. Inclusion of SPM or Chol in POPC membranes had different effects. Whereas SPM sustained pore formation, Chol promoted fusion activity. Even if partitioning into membranes was not affected in the absence of both SPM and Chol, HIV c had virtually no effect on POPC vesicles. Conditions described to disturb occurrence of lateral separation of phases in these systems reproduced the high peptidedose requirements for leakage as found in pure POPC vesicles and inhibited fusion. Surface aggregation assays using rhodamine-labeled peptides demonstrated that SPM and Chol promoted HIV c self-aggregation in membranes. Employing head-group fluorescent phospholipid analogs in planar supported lipid layers, we were able to discern HIV c clusters associated to ordered domains. Our results support the notion that the pretransmembrane sequence may participate in the clustering of gp41 monomers within the HIV-1 envelope, and in bilayer architecture destabilization at the loci of fusion.

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Section: Discussionmentioning

confidence: 99%

Section: Analysis Of Leakage Viamentioning

confidence: 99%

Sphingomyelin and Cholesterol Promote HIV-1 gp41 Pretransmembrane Sequence Surface Aggregation and Membrane Restructuring

Sáez‐Cirión

Nir

Lorizate

et al. 2002

Journal of Biological Chemistry

Self Cite

122

136

View full text Add to dashboard Cite

show abstract

“…The integrity of the liposome membranes was established according to reported procedures. [14] The efflux of chloride ion was monitored as a function of time using an Accumet glass-bodied chloride-selective electrode in conjunction with a Jenco multimeter. The results of the transport studies are summarized in Figure 3.…”

mentioning

confidence: 99%

Synthesis, Anion‐Binding Properties, and In Vitro Anticancer Activity of Prodigiosin Analogues

et al. 2005

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“…The fluorescent dye leakage assay is a well established method for the study of pore formation in membranes (34,35). Fig.…”

Section: Resultsmentioning

confidence: 99%

Structure of a Membrane-binding Domain from a Non-enveloped Animal Virus

Maia

Soares

Valente

et al. 2006

Journal of Biological Chemistry

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The ␥ 1 -peptide is a 21-residue lipid-binding domain from the non-enveloped Flock House virus (FHV). Unlike enveloped viruses, the entry of non-enveloped viruses into cells is believed to occur without membrane fusion. In this study, we performed NMR experiments to establish the solution structure of a membrane-binding peptide from a small non-enveloped icosahedral virus. The three-dimensional structure of the FHV ␥ 1 -domain was determined at pH 6.5 and 4.0 in a hydrophobic environment. The secondary and tertiary structures were evaluated in the context of the capacity of the peptide for permeabilizing membrane vesicles of different lipid composition, as measured by fluorescence assays. At both pH values, the peptide has a kinked structure, similar to the fusion domain from the enveloped viruses. The secondary structure was similar in three different hydrophobic environments as follows: water/trifluoroethanol, SDS, and membrane vesicles of different compositions. The ability of the peptide to induce vesicle leakage was highly dependent on the membrane composition. Although the ␥-peptide shares some structural properties to fusion domains of enveloped viruses, it did not induce membrane fusion. Our results suggest that small protein components such as the ␥-peptide in nodaviruses (such as FHV) and VP4 in picornaviruses have a crucial role in conducting nucleic acids through cellular membranes and that their structures resemble the fusion domains of membrane proteins from enveloped viruses.

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Effect of Phospholipid Composition on an Amphipathic Peptide-Mediated Pore Formation in Bilayer Vesicles

Cited by 59 publications

References 68 publications

Sphingomyelin and Cholesterol Promote HIV-1 gp41 Pretransmembrane Sequence Surface Aggregation and Membrane Restructuring

Sphingomyelin and Cholesterol Promote HIV-1 gp41 Pretransmembrane Sequence Surface Aggregation and Membrane Restructuring

Synthesis, Anion‐Binding Properties, and In Vitro Anticancer Activity of Prodigiosin Analogues

Structure of a Membrane-binding Domain from a Non-enveloped Animal Virus

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