Permeability properties of the membrane of vesicular stomatitis virions

Bittman, Robert; Majuk, Zenowij; Honig, Dan S.; Compans, Richard W.; Lenard, John

doi:10.1016/0005-2736(76)90178-4

Cited by 20 publications

(7 citation statements)

References 30 publications

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“…This result is in agreement with numerous studies on the behavior of nystatin in model and natural membranes (reviewed in refs. 21 and 22) and the studies of Bittman and coworkers (16) in particular. These investigators reported that filipin, another polyene antibiotic and channel former, also prevented osmotic swelling of vesicular stomatitis virus.…”

Section: Discussionmentioning

confidence: 95%

Disassembly of viral membranes by complement independent of channel formation.

Esser¹,

Bartholomew²,

Jensen³

et al. 1979

Proc. Natl. Acad. Sci. U.S.A.

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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 mo hology, integ- (2), who measured the release of radiolabeled RNA from mouse leukemia viruses (retroviruses). Later experiments with retroviruses indicated that human complement alone, without specific antibody, could lyse retroviruses (3-5). The mechanism of lysis of enveloped viruses was assumed to be similar or identical to complement-mediated lysis of mammalian cells, a more extensively studied and better understood reaction.In complement-dependent cytolysis, five complement proteins-C5b, C6, C7, C8, and C9-become physically attached to the outer membrane of a cell. Without further enzymatic modification, these proteins form a multimolecular complex, the membrane attack complex (MAC), that lyses cells by purely physicochemical means (reviewed in ref. 6). Loss of the natural impermeability of the cell membrane to small solutes leads to colloid-osmotic swelling of the cell, rupture, and release of internal proteins. Mayer (7,8) theorized that the MAC forms hydrophilic protein channels; this action is reminiscent of the channel-forming (9) and hemolytic (10) properties of the antibiotics nystatin and amphotericin B.In contrast to Mayer's channel theory, we recently proposed (11, 12) that the MAC is membranolytic not because of channel formation, but because of its strong phospholipid binding capacity, through which it is enabled to reorient the lipid bilayer structure of membranes.Examining our hypothesis, we have compared the effects of nystatin, melittin, and the MAC on the envelope of murine leukemia virus (MuLV) to determine if channel formation alone is sufficient to cause membranolysis. Nystatin is a channel former and melittin is not, although it is membranolytic. Our results show that whereas the MAC and melittin are virolytic, nystatin has no effect on the morphology and infectivity of the virus.MATERIALS AND METHODS Materials. Nystatin, amphotericin B, and melittin were purchased from Sigma. Rauscher MuLV, prepared by Electro-Nucleonics (Bethesda, MD), was supplied by the Office of Program Resources and Logistics, Viral Oncology, National Cancer Institute. Freshly harvested Moloney, xenotropic (ATS-124) murine, and (BN-p 454-9) rat leukemia viruses were propagated as described (6). Fresh human serum (Community Blood and Plasma, San Diego, CA) frozen at -70'C was used as a source of complement.Uranyl formate was prepared according to published procedures (13); all other chemicals were of the best grade commercially available. Buffer osmolarities were measured with a freezing-point depression osmometer (Osmette, Precision Systems, Sudbury, MA).Virolysis Assays. Virus samples (100,ug or approximately 1010 virions ...

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Section: Discussionmentioning

confidence: 95%

Disassembly of viral membranes by complement independent of channel formation.

Esser¹,

Bartholomew²,

Jensen³

et al. 1979

Proc. Natl. Acad. Sci. U.S.A.

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“…This sensitivity to laboratory proceedings is sometimes also reflected in viral properties after different purification procedures. Experiments with vesicular stomatitis virus and preliminary experiments with simian virus 5 (SV5; parainfluenza virus 5) and influenza virus indicated that the viruses appropriately swelled or shrank with the change in the osmolarity of the external media (3). Below are discussed the data that show that damaged Sendai virus uncoats in a process that is different from that used by intact virus.…”

Section: Membrane Uncoating Of Paramyxovirusesmentioning

confidence: 94%

Membrane Uncoating of Intact Enveloped Viruses

Haywood

2010

J Virol

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Experiments in the 1960s showed that Sendai virus, a paramyxovirus, fused its membrane with the host plasma membrane. After membrane fusion, the virus spontaneously "uncoated" with diffusion of the viral membrane proteins into the host plasma membrane and a merging of the host and viral membranes. This led to deposit of the viral ribonucleoprotein (RNP) and interior proteins in the cell cytoplasm. Later work showed that the common procedure then used to grow Sendai virus produced damaged, pleomorphic virions. Virions, which were grown under conditions that were not damaging, made a connecting structure between virus and cell at the region where the fusion occurred. The virus did not release its membrane proteins into the host membrane. The viral RNP was seen in the connecting structure in some cases. Uncoating of intact Sendai virus proceeds differently from uncoating described by the current standard model developed long ago with damaged virus. A model of intact paramyxovirus uncoating is presented and compared to what is known about the uncoating of other viruses.

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“…Changes in liposome volumes arising from shrinking and swelling were measured beginning at 150 ms after mixing. Measurements at shorter times were precluded by an artifact discussed elsewhere [e.g., Bittman et al (1976) and Owen & Eyring (1 975)]. The transmittance (T) following the 150-ms disturbance period was linear with respect to time, and the oscilloscope traces were similar to those shown previously for osmotic shrinking and swelling (Bittman & Blau, 1972).…”

Section: Efflux Of Trapped [14c]clucosementioning

confidence: 97%

Permeability properties of sterol-containing liposomes from analogs of phosphatidylcholine lacking acyl groups

Clejan¹,

Bittman²,

Deroo³

et al. 1979

Biochemistry

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The effect of sterols on the rates of nonelectrolyte movement in multilayered liposomal membranes formed from various phosphatidylcholine (PC) analogues was studied. We measured the temperature dependence of the permeation of small, polar solutes through lipid bilayers in the liquidcrystalline state of the following saturated phosphatidylcholines: diesters containing 14, 16, or 18 carbon atoms in each acyl chain; the corresponding diethers, which lack the carbonyl groups; and alkyl analogues, such as 2-octadecyleicosylphosphorylcholine (OEPC), which have no diacylglycerol or glycerol diether moiety. In addition, a diether-PC having one saturated and one unsaturated chain was used, and analogues of OEPC were synthesized in which the choline group is modified. At temperatures above the gel to liquid-crystalline phase transition of these diester, diether, and alkyl analogues of PC, the 30-hydroxysteroids cholesterol and ergosterol decreased the permeability of glycerol, urea, acetamide, and glucose, whereas epicholesterol and lanosterol exerted little effect on the reflection coefficient for acetamide penetration. Cholesterol reduced solute permeability in liposomes from OEPC analogues having increased separation

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Permeability properties of the membrane of vesicular stomatitis virions

Cited by 20 publications

References 30 publications

Disassembly of viral membranes by complement independent of channel formation.

Disassembly of viral membranes by complement independent of channel formation.

Membrane Uncoating of Intact Enveloped Viruses

Permeability properties of sterol-containing liposomes from analogs of phosphatidylcholine lacking acyl groups

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