Literature DB >> 19759132

Fusion between perinuclear virions and the outer nuclear membrane requires the fusogenic activity of herpes simplex virus gB.

Catherine C Wright1, Todd W Wisner, Brian P Hannah, Roselyn J Eisenberg, Gary H Cohen, David C Johnson.   

Abstract

Herpesviruses cross nuclear membranes (NMs) in two steps, as follows: (i) capsids assemble and bud through the inner NM into the perinuclear space, producing enveloped virus particles, and (ii) the envelopes of these virus particles fuse with the outer NM. Two herpes simplex virus (HSV) glycoproteins, gB and gH (the latter, likely complexed as a heterodimer with gL), are necessary for the second step of this process. Mutants lacking both gB and gH accumulate in the perinuclear space or in herniations (membrane vesicles derived from the inner NM). Both gB and gH/gL are also known to act directly in fusing the virion envelope with host cell membranes during HSV entry into cells, i.e., both glycoproteins appear to function directly in different aspects of the membrane fusion process. We hypothesized that HSV gB and gH/gL also act directly in the membrane fusion that occurs during virus egress from the nucleus. Previous studies of the role of gB and gH/gL in nuclear egress involved HSV gB and gH null mutants that could potentially also possess gross defects in the virion envelope. Here, we produced recombinant HSV-expressing mutant forms of gB with single amino acid substitutions in the hydrophobic "fusion loops." These fusion loops are thought to play a direct role in membrane fusion by insertion into cellular membranes. HSV recombinants expressing gB with any one of four fusion loop mutations (W174R, W174Y, Y179K, and A261D) were unable to enter cells. Moreover, two of the mutants, W174Y and Y179K, displayed reduced abilities to mediate HSV cell-to-cell spread, and W174R and A261D exhibited no spread. All mutant viruses exhibited defects in nuclear egress, enveloped virions accumulated in herniations and in the perinuclear space, and fewer enveloped virions were detected on cell surfaces. These results support the hypothesis that gB functions directly to mediate the fusion between perinuclear virus particles and the outer NM.

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Year:  2009        PMID: 19759132      PMCID: PMC2772685          DOI: 10.1128/JVI.01397-09

Source DB:  PubMed          Journal:  J Virol        ISSN: 0022-538X            Impact factor:   5.103


  45 in total

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Authors:  T Wisner; C Brunetti; K Dingwell; D C Johnson
Journal:  J Virol       Date:  2000-03       Impact factor: 5.103

Review 2.  Herpesvirus assembly and egress.

Authors:  Thomas C Mettenleiter
Journal:  J Virol       Date:  2002-02       Impact factor: 5.103

Review 3.  Directed egress of animal viruses promotes cell-to-cell spread.

Authors:  David C Johnson; Mary T Huber
Journal:  J Virol       Date:  2002-01       Impact factor: 5.103

4.  Herpes simplex virus glycoproteins gD and gE/gI serve essential but redundant functions during acquisition of the virion envelope in the cytoplasm.

Authors:  Aaron Farnsworth; Kimberly Goldsmith; David C Johnson
Journal:  J Virol       Date:  2003-08       Impact factor: 5.103

5.  Herpes simplex virus glycoprotein B associates with target membranes via its fusion loops.

Authors:  Brian P Hannah; Tina M Cairns; Florent C Bender; J Charles Whitbeck; Huan Lou; Roselyn J Eisenberg; Gary H Cohen
Journal:  J Virol       Date:  2009-04-15       Impact factor: 5.103

Review 6.  Herpesvirus entry: an update.

Authors:  Patricia G Spear; Richard Longnecker
Journal:  J Virol       Date:  2003-10       Impact factor: 5.103

7.  Localization of discontinuous epitopes of herpes simplex virus glycoprotein D: use of a nondenaturing ("native" gel) system of polyacrylamide gel electrophoresis coupled with Western blotting.

Authors:  G H Cohen; V J Isola; J Kuhns; P W Berman; R J Eisenberg
Journal:  J Virol       Date:  1986-10       Impact factor: 5.103

8.  Role of glycoprotein B of herpes simplex virus type 1 in viral entry and cell fusion.

Authors:  W H Cai; B Gu; S Person
Journal:  J Virol       Date:  1988-08       Impact factor: 5.103

9.  A herpes simplex virus mutant in which glycoprotein D sequences are replaced by beta-galactosidase sequences binds to but is unable to penetrate into cells.

Authors:  M W Ligas; D C Johnson
Journal:  J Virol       Date:  1988-05       Impact factor: 5.103

10.  Normal keratinization in a spontaneously immortalized aneuploid human keratinocyte cell line.

Authors:  P Boukamp; R T Petrussevska; D Breitkreutz; J Hornung; A Markham; N E Fusenig
Journal:  J Cell Biol       Date:  1988-03       Impact factor: 10.539

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  25 in total

1.  Characterisation of the epitope for a herpes simplex virus glycoprotein B-specific monoclonal antibody with high protective capacity.

Authors:  Martin P Däumer; Beate Schneider; Doris M Giesen; Sheriff Aziz; Rolf Kaiser; Bernd Kupfer; Karl E Schneweis; Jens Schneider-Mergener; Ulrich Reineke; Bertfried Matz; Anna M Eis-Hübinger
Journal:  Med Microbiol Immunol       Date:  2010-10-08       Impact factor: 3.402

2.  Dual split protein-based fusion assay reveals that mutations to herpes simplex virus (HSV) glycoprotein gB alter the kinetics of cell-cell fusion induced by HSV entry glycoproteins.

Authors:  Doina Atanasiu; Wan Ting Saw; John R Gallagher; Brian P Hannah; Zene Matsuda; J Charles Whitbeck; Gary H Cohen; Roselyn J Eisenberg
Journal:  J Virol       Date:  2013-08-14       Impact factor: 5.103

3.  Regulation of Herpes Simplex Virus Glycoprotein-Induced Cascade of Events Governing Cell-Cell Fusion.

Authors:  Doina Atanasiu; Wan Ting Saw; Roselyn J Eisenberg; Gary H Cohen
Journal:  J Virol       Date:  2016-11-14       Impact factor: 5.103

Review 4.  Herpesviruses remodel host membranes for virus egress.

Authors:  David C Johnson; Joel D Baines
Journal:  Nat Rev Microbiol       Date:  2011-05       Impact factor: 60.633

5.  Bimolecular complementation defines functional regions of Herpes simplex virus gB that are involved with gH/gL as a necessary step leading to cell fusion.

Authors:  Doina Atanasiu; J Charles Whitbeck; Manuel Ponce de Leon; Huan Lou; Brian P Hannah; Gary H Cohen; Roselyn J Eisenberg
Journal:  J Virol       Date:  2010-02-03       Impact factor: 5.103

6.  Low-pH-dependent changes in the conformation and oligomeric state of the prefusion form of herpes simplex virus glycoprotein B are separable from fusion activity.

Authors:  Stephen J Dollery; Catherine C Wright; David C Johnson; Anthony V Nicola
Journal:  J Virol       Date:  2011-08-03       Impact factor: 5.103

7.  Herpes simplex virus glycoproteins gB and gD function in a redundant fashion to promote secondary envelopment.

Authors:  David C Johnson; Todd W Wisner; Catherine C Wright
Journal:  J Virol       Date:  2011-03-16       Impact factor: 5.103

8.  Nuclear Exodus: Herpesviruses Lead the Way.

Authors:  Janna M Bigalke; Ekaterina E Heldwein
Journal:  Annu Rev Virol       Date:  2016-07-22       Impact factor: 10.431

9.  Mechanism of neutralization of herpes simplex virus by antibodies directed at the fusion domain of glycoprotein B.

Authors:  Tina M Cairns; Juan Fontana; Zhen-Yu Huang; J Charles Whitbeck; Doina Atanasiu; Samhita Rao; Spencer S Shelly; Huan Lou; Manuel Ponce de Leon; Alasdair C Steven; Roselyn J Eisenberg; Gary H Cohen
Journal:  J Virol       Date:  2013-12-18       Impact factor: 5.103

10.  Extended Synaptotagmin 1 Interacts with Herpes Simplex Virus 1 Glycoprotein M and Negatively Modulates Virus-Induced Membrane Fusion.

Authors:  Imane El Kasmi; Bita Khadivjam; Miki Lackman; Johanne Duron; Eric Bonneil; Pierre Thibault; Roger Lippé
Journal:  J Virol       Date:  2017-12-14       Impact factor: 5.103

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