Literature DB >> 7690263

Enhancement of viral fusion by nonadsorbing polymers.

A Herrmann1, M J Clague, R Blumenthal.   

Abstract

Nonadsorbing polymers such as dextran and poly(ethylene glycol) enhance binding as well as extents of fusion of influenza virus with erythrocytes. Kinetics and extent of viral membrane fusion were measured using an assay based on lipid mixing of a fluorescent dye. The effects of nonadsorbing polymers were in the concentration range from 0 to 10 wt%, far below the concentration required to overcome hydration repulsion forces. The enhancing effects were dependent on the molecular weight of nonadsorbing polymer, and only occurred at molecular weight > 1500; this links the phenomena we observe to the so-called "excluded volume effect" of nonadsorbing polymers. The time delay between triggering and the onset of influenza virus fusion was significantly reduced in the presence of nonadsorbing polymers. High molecular weight poly(ethylene glycol) also induced fusion of vesicular stomatitis virus with intact erythrocytes, which do not serve as target of vesicular stomatitis virus fusion in the absence of the polymer. The forces between membranes which determine rate-limiting processes in viral fusion and how they are affected by nonadsorbing polymers are discussed.

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Year:  1993        PMID: 7690263      PMCID: PMC1225745          DOI: 10.1016/S0006-3495(93)81054-3

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  32 in total

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Authors:  R Blumenthal; C Schoch; A Puri; M J Clague
Journal:  Ann N Y Acad Sci       Date:  1991       Impact factor: 5.691

2.  Delay time for influenza virus hemagglutinin-induced membrane fusion depends on hemagglutinin surface density.

Authors:  M J Clague; C Schoch; R Blumenthal
Journal:  J Virol       Date:  1991-05       Impact factor: 5.103

3.  Changes in the conformation of influenza virus hemagglutinin at the pH optimum of virus-mediated membrane fusion.

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Journal:  Proc Natl Acad Sci U S A       Date:  1982-02       Impact factor: 11.205

4.  Mechanism of poly(ethylene glycol)-induced lipid transfer between phosphatidylcholine large unilamellar vesicles: a fluorescent probe study.

Authors:  J R Wu; B R Lentz
Journal:  Biochemistry       Date:  1991-07-09       Impact factor: 3.162

5.  A long-lived state for influenza virus-erythrocyte complexes committed to fusion at neutral pH.

Authors:  C Schoch; R Blumenthal; M J Clague
Journal:  FEBS Lett       Date:  1992-10-26       Impact factor: 4.124

6.  Mechanism of precipitation of proteins by polyethylene glycols. Analysis in terms of excluded volume.

Authors:  D H Atha; K C Ingham
Journal:  J Biol Chem       Date:  1981-12-10       Impact factor: 5.157

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Authors:  M J Gething; J Sambrook
Journal:  Nature       Date:  1981-10-22       Impact factor: 49.962

8.  Role of target membrane structure in fusion with influenza virus: effect of modulating erythrocyte transbilayer phospholipid distribution.

Authors:  A Herrmann; M J Clague; R Blumenthal
Journal:  Membr Biochem       Date:  1993 Jan-Mar

9.  The interaction of phospholipid membranes with poly(ethylene glycol). Vesicle aggregation and lipid exchange.

Authors:  C P Tilcock; D Fisher
Journal:  Biochim Biophys Acta       Date:  1982-06-14

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Authors:  T Stegmann; J M White; A Helenius
Journal:  EMBO J       Date:  1990-12       Impact factor: 11.598

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  8 in total

1.  Conformational intermediates and fusion activity of influenza virus hemagglutinin.

Authors:  T Korte; K Ludwig; F P Booy; R Blumenthal; A Herrmann
Journal:  J Virol       Date:  1999-06       Impact factor: 5.103

2.  Epstein-Barr virus lacking glycoprotein gp42 can bind to B cells but is not able to infect.

Authors:  X Wang; L M Hutt-Fletcher
Journal:  J Virol       Date:  1998-01       Impact factor: 5.103

3.  Structural studies on membrane-embedded influenza hemagglutinin and its fragments.

Authors:  C Gray; L K Tamm
Journal:  Protein Sci       Date:  1997-09       Impact factor: 6.725

4.  Analysis of delay times of hemagglutinin-mediated fusion between influenza virus and cell membranes.

Authors:  K Ludwig; T Korte; A Herrmann
Journal:  Eur Biophys J       Date:  1995       Impact factor: 1.733

5.  pH-dependent binding of the fluorophore bis-ANS to influenza virus reflects the conformational change of hemagglutinin.

Authors:  T Korte; A Herrmann
Journal:  Eur Biophys J       Date:  1994       Impact factor: 1.733

6.  Changes in the lipid dynamics of liposomal membranes induced by poly(ethylene glycol): free volume alterations revealed by inter- and intramolecular excimer-forming phospholipid analogs.

Authors:  J Y Lehtonen; P K Kinnunen
Journal:  Biophys J       Date:  1994-06       Impact factor: 4.033

7.  Conformational change of influenza virus hemagglutinin is sensitive to ionic concentration.

Authors:  Thomas Korte; Kai Ludwig; Qiang Huang; P Sivaramakrishna Rachakonda; Andreas Herrmann
Journal:  Eur Biophys J       Date:  2007-01-09       Impact factor: 2.095

8.  Dilation of the influenza hemagglutinin fusion pore revealed by the kinetics of individual cell-cell fusion events.

Authors:  R Blumenthal; D P Sarkar; S Durell; D E Howard; S J Morris
Journal:  J Cell Biol       Date:  1996-10       Impact factor: 10.539

  8 in total

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