Kinetics of divalent cation induced fusion of phosphatidylserine vesicles: correlation between fusogenic capacities and binding affinities

Bentz, Joe; Düzgüne, Nejat; Nir, Shlomo

doi:10.1021/bi00283a004

Cited by 114 publications

(96 citation statements)

References 48 publications

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“…In conclusion, the amino-terminal peptide of the S protein has been shown to induce aggregation, close apposition of membranes and destabilization of the bilayers, the essential steps required for fusion (Bentz et al, 1983). These results support the idea that this region of the S protein plays an active role in the viral fusogenic processes and, then, might be considered as an important target in the design of immunological strategies for the prevention of HBV infection in vivo.…”

Section: Discussionsupporting

confidence: 67%

Phospholipid interactions of the putative fusion peptide of hepatitis B virus surface antigen S protein

Rodrı́guez-Crespo

Núñez

Gómez-Gutiérrez

et al. 1995

Journal of General Virology

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One of the first steps in the infective cycle of an enveloped virus consists of the fusion of the viral and cellular membranes. This process is usually achieved as a result of membrane destabilization brought about by a viral fusion peptide located at the amino terminus of one of the viral envelope glycoproteins. Previous sequence similarity studies by Rodrlguez-Crespo et al. (Journal of General Virology 75, 637-639, 1994) have shown that a hydrophobic stretch in the amino-terminal sequence of the S protein of hepatitis B virus shares several characteristics with fusion peptides of retroviruses and paramyxoviruses. A 16 residue peptide with this sequence was synthesized and its interaction with liposomes characterized. This peptide was able to mediate vesicle aggregation, lipid mixing and liposome leakage in a pH dependent manner at concentrations ranging from 3"5 to 52.0 pM. These effects were specific for negatively charged phospholipid vesicles. The peptide was also able to haemolyse erythrocytes. This study supports the notion that the sequence might be important in the initial infective steps of this virus, interacting with the target membranes and bringing about their subsequent destabilization.

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Section: Discussionsupporting

confidence: 67%

Phospholipid interactions of the putative fusion peptide of hepatitis B virus surface antigen S protein

Rodrı́guez-Crespo

Núñez

Gómez-Gutiérrez

et al. 1995

Journal of General Virology

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“…Alternatively, some triggering charges might be contributed by negatively charged phosphatidylserine, which is very abundant at the inner leaflet of the plasma membrane and can coordinate calcium ions (Martín-Molina et al, 2012). Indeed, it is well known that Ca 2+ can fuse protein-free phosphatidylserine vesicles, whereas the ability of Mg 2+ to do so is much lower (Bentz et al, 1983).…”

Section: Discussionmentioning

confidence: 99%

An Electrostatic Energy Barrier for SNARE-Dependent Spontaneous and Evoked Synaptic Transmission

et al. 2019

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Graphical Abstract Highlights d The energy barrier for vesicle fusion depends on SNAREcomplex surface charge d Positive charges decrease and negative charges increase the energy barrier for fusion d Addition of 35 positive charges per SNARE-complex fuses vesicles with evoked rates d Synaptotagmin-1 acts as an electrostatic switch, adding 18 charges by binding to Ca 2+ SUMMARYInformation transfer across CNS synapses depends on the very low basal vesicle fusion rate and the ability to rapidly upregulate that rate upon Ca 2+ influx. We show that local electrostatic repulsion participates in creating an energy barrier, which limits spontaneous synaptic transmission. The barrier amplitude is increased by negative charges and decreased by positive charges on the SNAREcomplex surface. Strikingly, the effect of charges on the barrier is additive and this extends to evoked transmission, but with a shallower charge dependence. Action potential-driven synaptic release is equivalent to the abrupt addition of $35 positive charges to the fusion machine. Within an electrostatic model for triggering, the Ca 2+ sensor synaptotagmin-1 contributes $18 charges by binding Ca 2+ , while also modulating the fusion barrier at rest. Thus, the energy barrier for synaptic vesicle fusion has a large electrostatic component, allowing synaptotagmin-1 to act as an electrostatic switch and modulator to trigger vesicle fusion.

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“…The dissociation factor intends to compensate for the leakage of aqueous contents that occurs shortly after the start of fusion. It is estimated by the sum of ‘ F +0.5 D ’ ( F : fusion fluorescence signal, D : dissociation signal from the pre‐encapsulated probes), as described by Bentz et al [16].…”

Section: Methodsmentioning

confidence: 99%

Diacylglycerol effects on phosphatidylinositol‐specific phospholipase C activity and vesicle fusion

2001

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Diacylglycerol increased the hydrolytic activity of phosphatidylinositol-specific phospholipase C on large unilamellar vesicles containing 5^40% phosphatidylinositol. Moreover, diacylglycerol increased the rate and extent of vesicle fusion (contents mixing) induced by the enzyme. Kinetic studies of intervesicular lipid mixing revealed that fusion was limited by the frequency of contacts involving two diacylglycerol-rich domains. ß

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Kinetics of divalent cation induced fusion of phosphatidylserine vesicles: correlation between fusogenic capacities and binding affinities

Cited by 114 publications

References 48 publications

Phospholipid interactions of the putative fusion peptide of hepatitis B virus surface antigen S protein

Phospholipid interactions of the putative fusion peptide of hepatitis B virus surface antigen S protein

An Electrostatic Energy Barrier for SNARE-Dependent Spontaneous and Evoked Synaptic Transmission

Diacylglycerol effects on phosphatidylinositol‐specific phospholipase C activity and vesicle fusion

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