NDLI: Disassembly of viral membranes by complement independent of channel formation.

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Distinctive nucleotide sequences of promoters recognized by RNA polymerase containing a phage-coded "sigma-like" protein.

Altered promoter selection by a novel form of Bacillus subtilis RNA polymerase.

Extracts of Drosophila embryos mediate chromatin assembly in vitro.

Evidence for hydrophobic region within heavy chains of mouse B lymphocyte membrane-bound IgM.

Attenuation in the Escherichia coli tryptophan operon: role of RNA secondary structure involving the tryptophan codon region.

Termination of transcription in nucleoli isolated from Tetrahymena.

Amino acid sequence of an immunoglobulin-like HLA antigen heavy chain domain.

Effect of interchain disulfide bond on hapten binding properties of light chain dimer of protein 315.

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Neoplastic transformation of epithelial cells in whole mammary gland in vitro.

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Biochemical and morphologic studies on diabetic rats: effects of sucrose-enriched diet in rats with pancreatic islet transplants.

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Properties and localization of beta-endorphin receptor in rat brain.

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Disassembly of viral membranes by complement independent of channel formation.

Structural characterization of the murine fourth component of complement and sex-limited protein and their precursors: evidence for two loci in the S region of the H-2 complex.

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Disassembly of viral membranes by complement independent of channel formation.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Jensen, F. C. Bartholomew, R. M. Esser, A. F. Müller-eberhard, H. J.
Abstract	We have compared the effects of the complement membrane attack complex (MAC), nystatin, and melittin on the envelope of murine leukemia viruses to determine if channel formation alone is sufficient to cause membranolysis. Nystatin is a channel former and mellitin is not, although both are hemolytic. Whereas MAC and melittin disintegrated the viral membrane, nystatin had no effect on morphology, integrity, and infectivity of the virus. Incorporation of the antibiotic into the viral membranes was demonstrated by measurements of the characteristic fluorescence of nystatin in membranes and the dose-dependent increase in viral density after uptake of the antibiotic. The density of nystatin was measured to be 1.26-1.27 g/cm3. Proof for the formation of functional nystatin channels was obtained by light scattering measurements. Exposure of untreated virus to hypotonic conditions increased viral light scattering because of osmotic swelling but otherwise had no effect on the integrity of the virus. Nystatin channel formation abolished the light scattering change, showing that the antibiotic had impaired the viral permeability barrier. We interpret these results to indicate that virolysis by MAC is not caused by channel formation and, conversely, in the absence of colloid-osmotic effects, channel formation by itself is not sufficient to disassemble a viral membrane.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	11
Volume Number	76
Language	English
Publisher	National Academy of Sciences
Publisher Date	1979-01-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bee Venoms Pharmacology Complement System Proteins Metabolism Cytotoxicity, Immunologic Ion Channels Drug Effects Leukemia Virus, Murine Melitten Nystatin Animals Enzymology Membranes Mice Permeability RNA-Directed DNA Polymerase Water-Electrolyte Balance Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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