Cytolytic pore-forming proteins and peptides: is there a common structural motif?

Ojcius, David M.; Young, John D.

doi:10.1016/0968-0004(91)90090-i

Cited by 206 publications

(137 citation statements)

References 24 publications

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“…The radioactivity associated with microsomes was measured in vesicles incubated both in the presence and absence of the pore-forming antibiotic alamethicin (41,44) to determine net intravesicular accumulation. Because, in addition to [ 14 C]glucose-6-phosphate, [ 14 C]glucose (produced by glucose-6-phosphatase activity) can contribute to the intravesicular measured radioactivity (as it was indeed the case, see below), we expressed as "glucose-6-phosphate ϩ glucose" the 14 C-radioactivity accumulated (see Fig.…”

Section: Resultsmentioning

confidence: 99%

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Demonstration of a Metabolically Active Glucose-6-phosphate Pool in the Lumen of Liver Microsomal Vesicles

Bánhegyi

Marcolongo

Fulceri

et al. 1997

Journal of Biological Chemistry

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Glucose-6-phosphate transport was investigated in rat or human liver microsomal vesicles using rapid filtration and light-scattering methods. Upon addition of glucose-6-phosphate, rat liver microsomes accumulated the radioactive tracer, reaching a steady-state level of uptake. In this phase, the majority of the accumulated tracer was glucose, but a significant intraluminal glucose-6-phosphate pool could also be observed. The extent of the intravesicular glucose pool was proportional with glucose-6-phosphatase activity. The relative size of the intravesicular glucose-6-phosphate pool (irrespective of the concentration of the extravesicular concentration of added glucose-6-phosphate) expressed as the apparent intravesicular space of the hexose phosphate was inversely dependent on glucose-6-phosphatase activity. The increase of hydrolysis by elevating the extravesicular glucose-6-phosphate concentration or temperature resulted in lower apparent intravesicular glucose-6-phosphate spaces and, thus, in a higher transmembrane gradient of glucose-6-phosphate concentrations. In contrast, inhibition of glucose-6-phosphate hydrolysis by vanadate, inactivation of glucose-6-phosphatase by acidic pH, or genetically determined low or absent glucose-6-phosphatase activity in human hepatic microsomes of patients suffering from glycogen storage disease type 1a led to relatively high intravesicular glucose-6-phosphate levels. Glucose-6-phosphate transport investigated by light-scattering technique resulted in similar traces in control and vanadate-treated rat microsomes as well as in microsomes from human patients with glycogen storage disease type 1a. It is concluded that liver microsomes take up glucose-6-phosphate, constituting a pool directly accessible to intraluminal glucose-6-phosphatase activity. In addition, normal glucose-6-phosphate uptake can take place in the absence of the glucose-6-phosphatase enzyme protein, confirming the existence of separate transport proteins.

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Section: Resultsmentioning

confidence: 99%

“…In each experiment, alamethicin (0.05 mg/ml) was added to the parallel incubates to distinguish the intravesicular and the bound radioactivity (41,44). The alamethicin-permeabilized microsomes were recovered on filters and washed as above.…”

Section: Methodsmentioning

confidence: 99%

Demonstration of a Metabolically Active Glucose-6-phosphate Pool in the Lumen of Liver Microsomal Vesicles

Bánhegyi

Marcolongo

Fulceri

et al. 1997

Journal of Biological Chemistry

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“…Although it is pure speculation to date, one might assume that the E1 homo-oligomers could form a pore in a barrel-stave-like structure (Ojcius and Young, 1991). It is also conceivable that E, oligomers might constitute the SFV fusion pore (Lanzrein et al, 1993a), as it was shown that E1 is the subunit that catalyses fusion (Omar and Koblet, 1988).…”

Section: Do Alphavirus Proteins Have Channel Activities?mentioning

confidence: 99%

Entry and uncoating of enveloped viruses

Lanzrein

Schlegel

Kempf

1994

Biochemical Journal

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“…We then consider the case of a highly incompressible, but purely viscous membrane of varying porosity. Such systems are reminiscent of giant unilamellar vesicles (GUVs) [14,15,16] containing pore-forming proteins [17,18,19].…”

Section: Introductionmentioning

confidence: 99%

Nanorheology of viscoelastic shells: Applications to viral capsids

Kuriabova

Levine

2008

Phys. Rev. E

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We study the microrheology of nanoparticle shells [Dinsmore et al. Science 298, 1006(2002] and viral capsids [Ivanovska et al. PNAS 101, 7600 (2004)] by computing the mechanical response function and thermal fluctuation spectrum of a viscoelastic spherical shell that is permeable to the surrounding solvent. We determine analytically the damped dynamics of the shear, bend, and compression modes of the shell coupled to the solvent both inside and outside the sphere in the zero Reynolds number limit. We identify fundamental length and time scales in the system, and compute the thermal correlation function of displacements of antipodal points on the sphere and the mechanical response to pinching forces applied at these points. We describe how such a frequency-dependent antipodal correlation and/or response function, which should be measurable in new AFM-based microrheology experiments, can probe the viscoelasticity of these synthetic and biological shells constructed of nanoparticles.

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Cytolytic pore-forming proteins and peptides: is there a common structural motif?

Cited by 206 publications

References 24 publications

Demonstration of a Metabolically Active Glucose-6-phosphate Pool in the Lumen of Liver Microsomal Vesicles

Demonstration of a Metabolically Active Glucose-6-phosphate Pool in the Lumen of Liver Microsomal Vesicles

Entry and uncoating of enveloped viruses

Nanorheology of viscoelastic shells: Applications to viral capsids

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