In vitro characterization of EHV-4 gG-deleted mutant.
Abstract: Equine herpesvirus 4 (EHV-4) is an important pathogen that causes respiratory tract disease in horse populations worldwide. Glycoprotein G (gG) homologs have been identified in several alphaherpesviruses as minor non-essential membrane-anchored glycoproteins. In this study, EHV-4 gG deletion mutant has been generated by using bacterial artificial chromosome technology to investigate the role of gG in viral pathogenesis. Our findings reported here revealed no significant difference between parental EHV-4 and gG-negative strain in their replication cycle in cell culture. Furthermore, virus titers and plaque formation were comparable in both viruses. It is noteworthy that these findings disagree with the previously published study describing gG deletion in another EHV-4 strain.
Publication Date: 2011-09-29 PubMed ID: 21960433DOI: 10.1007/s11262-011-0677-6Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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This research focuses on the role of glycoprotein G (gG) in the pathogenesis of Equine herpesvirus 4, a common respiratory disease in horses. Through the use of bacterial artificial chromosome technology, the research revealed no significant difference in the replication cycle, virus titers, and plaque formation between the parental EHV-4 and the gG-deleted strain.
Objective of the Research
- This study aimed to investigate the role of glycoprotein G (gG) in the pathogenesis of Equine herpesvirus 4 (EHV-4), which is a respiratory disease prevalent worldwide amongst horses.
Methodology
- The researchers have employed bacterial artificial chromosome technology to generate an EHV-4 gG-deleted mutant. This is done to meticulously observe the disparity (if any), in the behaviour of the viral pathogen with its gG component removed.
Findings
- Despite the removal of the gG component, no significant differences were noted between the mutant and the parental EHV-4 strain in their replication cycle in the cell culture. This suggests that the presence or absence of gG might not necessarily affect the replication of this virus.
- On similar lines, the research observed no noticeable variance in their virus titers and plaque formation, implying that gG, although being an integral component, might not influence these aspects of the virus.
Conclusion
- Contrary to a previously published study, this research argues that gG’s removal does not significantly alter the behavior of the EHV-4 virus in terms of replication, virus titers, and plaque formation. However, more extensive studies are required to ascertain these findings since they counter existing literature.
Cite This Article
APA
Azab W, El-Sheikh A, Abdel-Gawad A.
(2011).
In vitro characterization of EHV-4 gG-deleted mutant.
Virus Genes, 44(1), 109-111.
https://doi.org/10.1007/s11262-011-0677-6 Publication
Researcher Affiliations
- Department of Virology, Zagazig University, Zagazig, Egypt. wfazab@zedat.fu-berlin.de
MeSH Terms
- Animals
- Herpesviridae Infections / veterinary
- Herpesviridae Infections / virology
- Herpesvirus 4, Equid / genetics
- Herpesvirus 4, Equid / pathogenicity
- Herpesvirus 4, Equid / physiology
- Horse Diseases / virology
- Horses
- Sequence Deletion
- Viral Envelope Proteins / genetics
- Viral Envelope Proteins / metabolism
- Virulence
- Virus Replication
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Citations
This article has been cited 3 times.- Losinno A, Vissani MA, Sanchez D, Damiani AM. Equid herpesvirus type 3 infection produces membrane-associated and secreted forms of glycoprotein G that are not required for efficient cell-to-cell spread of the virus in vitro. Arch Virol 2023 Mar 28;168(4):122.
- Azab W, El-Sheikh A. The role of equine herpesvirus type 4 glycoprotein k in virus replication. Viruses 2012 Aug;4(8):1258-63.
- Qiu J, Wang Z, Wang M, Cheng A, Yang Q, Ou X, Sun D, He Y, Tian B, Wu Z, Zhang S, Huang J, Wu Y, Zhao X, Zhu D, Chen S, Jia R, Liu M. Duck plague virus gG is secreted, nonstructural glycoprotein, not essential for viral replication and responsible for the virulence. Poult Sci 2025 Sep;104(9):105399.
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