(Q24604871)

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

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

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Roselyn J. Eisenberg

7

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Roselyn J Eisenberg

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6

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Gary H Cohen

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author name string

Doina Atanasiu

1

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J Charles Whitbeck

2

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Manuel Ponce de Leon

3

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Huan Lou

4

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Brian P Hannah

5

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publication date

April 2010

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Journal of Virology

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84

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8

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3825-34

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Bimolecular complementation of paramyxovirus fusion and hemagglutinin-neuraminidase proteins enhances fusion: implications for the mechanism of fusion triggering

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7 April 2017

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

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7 April 2017

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

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7 April 2017

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1 reference

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7 April 2017

Structure-based analysis of the herpes simplex virus glycoprotein D binding site present on herpesvirus entry mediator HveA (HVEM).

1 reference

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Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor

1 reference

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The postfusion structure of baculovirus gp64 supports a unified view of viral fusion machines

1 reference

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7 April 2017

Herpes simplex virus glycoprotein D bound to the human receptor HveA

1 reference

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1 reference

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7 April 2017

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

1 reference

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27 September 2017

Cross talk among the glycoproteins involved in herpes simplex virus entry and fusion: the interaction between gB and gH/gL does not necessarily require gD.

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Class III viral membrane fusion proteins

1 reference

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Human cytomegalovirus glycoproteins gB and gH/gL mediate epithelial cell-cell fusion when expressed either in cis or in trans

1 reference

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Entry of herpesviruses into mammalian cells

1 reference

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27 September 2017

Bimolecular fluorescence complementation: visualization of molecular interactions in living cells

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2849501

27 September 2017

Bimolecular complementation reveals that glycoproteins gB and gH/gL of herpes simplex virus interact with each other during cell fusion

1 reference

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27 September 2017

Complexes between herpes simplex virus glycoproteins gD, gB, and gH detected in cells by complementation of split enhanced green fluorescent protein

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2849501

27 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2849501

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Design and implementation of bimolecular fluorescence complementation (BiFC) assays for the visualization of protein interactions in living cells

1 reference

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Mutational evidence of internal fusion loops in herpes simplex virus glycoprotein B

1 reference

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Crystal structure of glycoprotein B from herpes simplex virus 1.

1 reference

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1 reference

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Structure of unliganded HSV gD reveals a mechanism for receptor-mediated activation of virus entry.

1 reference

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Herpes simplex virus glycoprotein B binds to cell surfaces independently of heparan sulfate and blocks virus entry

1 reference

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1 reference

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Use of herpes simplex virus and pseudorabies virus chimeric glycoprotein D molecules to identify regions critical for membrane fusion

1 reference

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Cell-surface expression of a mutated Epstein-Barr virus glycoprotein B allows fusion independent of other viral proteins

1 reference

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The soluble ectodomain of herpes simplex virus gD contains a membrane-proximal pro-fusion domain and suffices to mediate virus entry

1 reference

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1 reference

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Herpesvirus entry: an update

1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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Herpes simplex virus glycoprotein D can bind to poliovirus receptor-related protein 1 or herpesvirus entry mediator, two structurally unrelated mediators of virus entry

1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

https://pubmed.ncbi.nlm.nih.gov/20130048

12 December 2020

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10.1128/JVI.02687-09

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