The fusion loops and membrane proximal region of Epstein-Barr virus glycoprotein B (gB) can function in the context of herpes simplex virus 1 gB when substituted individually but not in combination

Anna Zago; Sarah A. Connolly; Patricia G. Spear; Richard Longnecker

doi:10.1016/j.virusres.2012.10.015

The fusion loops and membrane proximal region of Epstein-Barr virus glycoprotein B (gB) can function in the context of herpes simplex virus 1 gB when substituted individually but not in combination

Anna Zago, Sarah A. Connolly^*, Patricia G. Spear, Richard Longnecker

^*Corresponding author for this work

Microbiology-Immunology

Research output: Contribution to journal › Article › peer-review

2 Scopus citations

Abstract

Among the herpesvirus glycoprotein B (gB) fusion proteins, the hydrophobic content of fusion loops and membrane proximal regions (MPRs) are inversely correlated with each other. We examined the functional importance of the hydrophobicity of these regions by replacing them in herpes simplex virus type 1 gB with corresponding regions from Epstein-Barr virus gB. We show that fusion activity is dependent on the structural context in which the specific loops and MPR sequences exist, rather than a simple hydrophobic relationship.

Original language	English (US)
Pages (from-to)	227-230
Number of pages	4
Journal	Virus Research
Volume	171
Issue number	1
DOIs	https://doi.org/10.1016/j.virusres.2012.10.015
State	Published - Jan 2013

Keywords

Entry
Epstein-Barr virus
Fusion
Glycoprotein B
Herpes simplex virus

ASJC Scopus subject areas

Infectious Diseases
Cancer Research
Virology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.virusres.2012.10.015

Cite this

@article{333a7200be97454db6e51fa3fd4a8478,

title = "The fusion loops and membrane proximal region of Epstein-Barr virus glycoprotein B (gB) can function in the context of herpes simplex virus 1 gB when substituted individually but not in combination",

abstract = "Among the herpesvirus glycoprotein B (gB) fusion proteins, the hydrophobic content of fusion loops and membrane proximal regions (MPRs) are inversely correlated with each other. We examined the functional importance of the hydrophobicity of these regions by replacing them in herpes simplex virus type 1 gB with corresponding regions from Epstein-Barr virus gB. We show that fusion activity is dependent on the structural context in which the specific loops and MPR sequences exist, rather than a simple hydrophobic relationship.",

keywords = "Entry, Epstein-Barr virus, Fusion, Glycoprotein B, Herpes simplex virus",

author = "Anna Zago and Connolly, {Sarah A.} and Spear, {Patricia G.} and Richard Longnecker",

note = "Funding Information: We thank Nanette Susmarski for cell culture, Marija Backovic for alignments, and the members of the Spear and Longnecker laboratories for support. This work was supported by NIH grants CA021776 to PGS and RL and AI067048 to RL.",

year = "2013",

month = jan,

doi = "10.1016/j.virusres.2012.10.015",

language = "English (US)",

volume = "171",

pages = "227--230",

journal = "Virus Research",

issn = "0168-1702",

publisher = "Elsevier B.V.",

number = "1",

}

The fusion loops and membrane proximal region of Epstein-Barr virus glycoprotein B (gB) can function in the context of herpes simplex virus 1 gB when substituted individually but not in combination. / Zago, Anna; Connolly, Sarah A.; Spear, Patricia G. et al.
In: Virus Research, Vol. 171, No. 1, 01.2013, p. 227-230.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - The fusion loops and membrane proximal region of Epstein-Barr virus glycoprotein B (gB) can function in the context of herpes simplex virus 1 gB when substituted individually but not in combination

AU - Zago, Anna

AU - Connolly, Sarah A.

AU - Spear, Patricia G.

AU - Longnecker, Richard

N1 - Funding Information: We thank Nanette Susmarski for cell culture, Marija Backovic for alignments, and the members of the Spear and Longnecker laboratories for support. This work was supported by NIH grants CA021776 to PGS and RL and AI067048 to RL.

PY - 2013/1

Y1 - 2013/1

N2 - Among the herpesvirus glycoprotein B (gB) fusion proteins, the hydrophobic content of fusion loops and membrane proximal regions (MPRs) are inversely correlated with each other. We examined the functional importance of the hydrophobicity of these regions by replacing them in herpes simplex virus type 1 gB with corresponding regions from Epstein-Barr virus gB. We show that fusion activity is dependent on the structural context in which the specific loops and MPR sequences exist, rather than a simple hydrophobic relationship.

AB - Among the herpesvirus glycoprotein B (gB) fusion proteins, the hydrophobic content of fusion loops and membrane proximal regions (MPRs) are inversely correlated with each other. We examined the functional importance of the hydrophobicity of these regions by replacing them in herpes simplex virus type 1 gB with corresponding regions from Epstein-Barr virus gB. We show that fusion activity is dependent on the structural context in which the specific loops and MPR sequences exist, rather than a simple hydrophobic relationship.

KW - Entry

KW - Epstein-Barr virus

KW - Fusion

KW - Glycoprotein B

KW - Herpes simplex virus

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UR - http://www.scopus.com/inward/citedby.url?scp=84872810726&partnerID=8YFLogxK

U2 - 10.1016/j.virusres.2012.10.015

DO - 10.1016/j.virusres.2012.10.015

M3 - Article

C2 - 23089849

AN - SCOPUS:84872810726

SN - 0168-1702

VL - 171

SP - 227

EP - 230

JO - Virus Research

JF - Virus Research

IS - 1

ER -

The fusion loops and membrane proximal region of Epstein-Barr virus glycoprotein B (gB) can function in the context of herpes simplex virus 1 gB when substituted individually but not in combination

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

Access to Document

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