By D. Papahadjopoulos, G. Poste, W. J. Vail (auth.), Edward D. Korn (eds.)

ISBN-10: 1468409859

ISBN-13: 9781468409857

ISBN-10: 1468409875

ISBN-13: 9781468409871

Three articles make up quantity 10 of tools in Membrane Biology. within the first of those, Papahadjopoulos, Poste, and Vail broadly overview a lot of the to be had facts at the fusion of traditional membranes, version membranes (liposomes), and normal membranes with liposomes. The authors are led by means of their evaluation of the experimental equipment and their interpretations of the implications acquired to a common conception of membrane fusion which they think is acceptable to all platforms which have been studied. Arguing that even if protein and carbohydrate may well serve, on occasion, to carry membranes into sufficiently shut proximity for fusion to happen and, in different situations, to take away peripheral and crucial proteins from the areas which are to suffer fusion, the authors finish that membrane fusion in step with se is simply a estate of the lipid bilayer. of their view, all of the experimental observations to this point may be subsumed below a unifying speculation within which membrane fusion is the results of a section separation in one-half of the membrane bilayer led to through the interplay - of calcium ions with acidic phospholipids, ordinarily phosphatidylserine. the place half-membranes already include enough acidic phospholipids, an area raise in calcium ion focus may possibly suffice to urge fusion (examples may contain exocytosis and fusion of intracellular membrane systems). In different instances, average or experimentally caused occasions previous fusion will be essential to bring up the neighborhood focus of the acidic phospholipids within the half-membrane (virus-or fusogenic agent-induced cell-to-cell fusion, or endocytosis, for example).

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Extra info for Methods in Membrane Biology: Volume 10

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The creation of "artificial virus receptors" on the cell surface may, however, offer a potentially useful method for studying the functional properties of paramyxovirus envelope glycoproteins. As mentioned previously, evaluation of the cell fusion activity of virus particles lacking the HN glycoprotein has been hindered because of the failure of such particles to adsorb to cells. It might be of interest, therefore, to test whether virus particles lacking HN but containing the F glycoprotein (naturally occurring ts mutants, enzymically depleted particles, or reconstituted particles) could induce agglutination and fusion of lectin-treated erythrocytes.

The reasons for these differences 26 D. Papahadjopoulos, G. Poste, and W. J. Vail are not clear. , 1972) may affect cellular susceptibility to fusion. However, detailed information on the mechanism(s) by which these factors and other aspects of cell surface organization can influence the cell fusion reaction is still lacking. Cellular susceptibility to fusion is also influenced by a number of ill-defined factors such as cell passage level, the length of time since subcultivation before exposure to virus, and the stage in the cell cycle (see Poste, 1972).

Poste, and W. J. , 1972; Scheid and Choppin, 1973, 1975; Urata and Seto, 1975). , 1973). This protein is called the HN glycoprotein. The smaller envelope glycoprotein (molecular weight 53,000-56,000), referred to as the F (fusion) protein, is devoid of neuraminidase and hemagglutinating activities and is involved in virusinduced cell fusion and hemolysis. The clue that the ability of paramyxoviruses to induce FFWO was associated with the F glycoprotein came from studies in which the structural proteins of virions grown in different host cells were compared.

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Methods in Membrane Biology: Volume 10 by D. Papahadjopoulos, G. Poste, W. J. Vail (auth.), Edward D. Korn (eds.)

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