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Literature DB >> 17553877

Hydrophobic residues that form putative fusion loops of Epstein-Barr virus glycoprotein B are critical for fusion activity.

Marija Backovic¹, Theodore S Jardetzky, Richard Longnecker.

Abstract

To test the importance of the hydrophobic residues within the putative Epstein-Barr virus (EBV) glycoprotein B (gB) fusion loops in membrane fusion, WY(112-113) and WLIW(193-196) were mutated into alanine, glutamic acid, or the analogous residues from herpes simplex virus type 1 (HSV-1) gB (HR and RVEA). All gB variants exhibited cell surface expression, demonstrating that the substitutions did not perturb gB trafficking. None of six gB variants was, however, capable of mediating fusion with either epithelial or B cells. These data demonstrate that the bulky and hydrophobic EBV loop residues, which differ from the more hydrophilic HSV-1 residues and appear more compatible with membrane insertion, are essential for EBV gB-dependent fusion.

Entities: Chemical Disease Gene Species

Mesh：

Substances：

Year: 2007 PMID： 17553877 PMCID： PMC1951416 DOI： 10.1128/JVI.00758-07

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

35 in total

1. ESPript: analysis of multiple sequence alignments in PostScript.

Authors: P Gouet; E Courcelle; D I Stuart; F Métoz
Journal: Bioinformatics Date: 1999-04 Impact factor: 6.937

2. Soluble Epstein-Barr virus glycoproteins gH, gL, and gp42 form a 1:1:1 stable complex that acts like soluble gp42 in B-cell fusion but not in epithelial cell fusion.

Authors: Austin N Kirschner; Jasmina Omerovic; Boris Popov; Richard Longnecker; Theodore S Jardetzky
Journal: J Virol Date: 2006-10 Impact factor: 5.103

3. Characterization of human cytomegalovirus glycoprotein-induced cell-cell fusion.

Authors: Eric R Kinzler; Teresa Compton
Journal: J Virol Date: 2005-06 Impact factor: 5.103

4. Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G.

Authors: Stéphane Roche; Stéphane Bressanelli; Félix A Rey; Yves Gaudin
Journal: Science Date: 2006-07-14 Impact factor: 47.728

5. A simple method for displaying the hydropathic character of a protein.

Authors: J Kyte; R F Doolittle
Journal: J Mol Biol Date: 1982-05-05 Impact factor: 5.469

6. The amino terminus of Epstein-Barr virus glycoprotein gH is important for fusion with epithelial and B cells.

Authors: Jasmina Omerović; Lori Lev; Richard Longnecker
Journal: J Virol Date: 2005-10 Impact factor: 5.103

7. Resting B cells as a transfer vehicle for Epstein-Barr virus infection of epithelial cells.

Authors: C D Shannon-Lowe; B Neuhierl; G Baldwin; A B Rickinson; H-J Delecluse
Journal: Proc Natl Acad Sci U S A Date: 2006-04-10 Impact factor: 11.205

8. Herpes simplex virus type 1 mediates fusion through a hemifusion intermediate by sequential activity of glycoproteins D, H, L, and B.

Authors: Ravi P Subramanian; Robert J Geraghty
Journal: Proc Natl Acad Sci U S A Date: 2007-02-13 Impact factor: 11.205

9. Crystal structure of glycoprotein B from herpes simplex virus 1.

Authors: Ekaterina E Heldwein; Huan Lou; Florent C Bender; Gary H Cohen; Roselyn J Eisenberg; Stephen C Harrison
Journal: Science Date: 2006-07-14 Impact factor: 47.728

Review 10. Virus membrane-fusion proteins: more than one way to make a hairpin.

Authors: Margaret Kielian; Félix A Rey
Journal: Nat Rev Microbiol Date: 2006-01 Impact factor: 60.633

39 in total

1. Structure-based functional analyses of domains II and III of pseudorabies virus glycoprotein H.

Authors: Sebastian W Böhm; Elisa Eckroth; Marija Backovic; Barbara G Klupp; Felix A Rey; Thomas C Mettenleiter; Walter Fuchs
Journal: J Virol Date: 2014-11-12 Impact factor: 5.103

2. Residues within the C-terminal arm of the herpes simplex virus 1 glycoprotein B ectodomain contribute to its refolding during the fusion step of virus entry.

Authors: Sarah A Connolly; Richard Longnecker
Journal: J Virol Date: 2012-04-04 Impact factor: 5.103

Hydrophobic residues that form putative fusion loops of Epstein-Barr virus glycoprotein B are critical for fusion activity.

1. ESPript: analysis of multiple sequence alignments in PostScript.

2. Soluble Epstein-Barr virus glycoproteins gH, gL, and gp42 form a 1:1:1 stable complex that acts like soluble gp42 in B-cell fusion but not in epithelial cell fusion.

3. Characterization of human cytomegalovirus glycoprotein-induced cell-cell fusion.

4. Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G.

5. A simple method for displaying the hydropathic character of a protein.

6. The amino terminus of Epstein-Barr virus glycoprotein gH is important for fusion with epithelial and B cells.

7. Resting B cells as a transfer vehicle for Epstein-Barr virus infection of epithelial cells.

8. Herpes simplex virus type 1 mediates fusion through a hemifusion intermediate by sequential activity of glycoproteins D, H, L, and B.

9. Crystal structure of glycoprotein B from herpes simplex virus 1.

Review 10. Virus membrane-fusion proteins: more than one way to make a hairpin.

1. Structure-based functional analyses of domains II and III of pseudorabies virus glycoprotein H.

2. Residues within the C-terminal arm of the herpes simplex virus 1 glycoprotein B ectodomain contribute to its refolding during the fusion step of virus entry.

3. Characterization of EBV gB indicates properties of both class I and class II viral fusion proteins.

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

Review 5. Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme.

6. Mapping regions of Epstein-Barr virus (EBV) glycoprotein B (gB) important for fusion function with gH/gL.

7. Structure-based mutational analysis of the highly conserved domain IV of glycoprotein H of pseudorabies virus.

8. Analysis of Epstein-Barr virus glycoprotein B functional domains via linker insertion mutagenesis.

Review 9. Class III viral membrane fusion proteins.

Review 10. The structural basis of herpesvirus entry.