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Journal ArticleDOI

Construction and characterization of an equine herpesvirus 1 glycoprotein C negative mutant

Nikolaus Osterrieder
- 01 Feb 1999 - 
- Vol. 59, Iss: 2, pp 165-177
TLDR
Equine herpesvirus 1 (EHV-1) strain RacL 11 mutant was constructed that carries the Escherichia coli LacZ gene instead of the open reading frame encoding glycoprotein C (gC) and plays important roles in the early steps of infection and in release of virions, especially in primary equine cells, and contributes to EHV- 1 virulence.
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This article is published in Virus Research.The article was published on 1999-02-01. It has received 80 citations till now. The article focuses on the topics: Equine herpesvirus 1 & Virus.

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Citations
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Journal ArticleDOI

Horizontal transmission of Marek's disease virus requires US2, the UL13 protein kinase, and gC.

TL;DR: Reconstituted viruses based on pRB-1B showed that US2, UL13, and gC in combination are essential for horizontal transmission of MDV and that none of the genes alone is able to restore this phenotype.
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Equine herpesviruses type 1 (EHV-1) and 4 (EHV-4)--masters of co-evolution and a constant threat to equids and beyond.

TL;DR: Understanding the equine herpesviruses' repertoire of immunomodulatory mechanisms may lead the way to develop more efficient vaccines.
Journal ArticleDOI

Multivalent Flexible Nanogels Exhibit Broad-Spectrum Antiviral Activity by Blocking Virus Entry.

TL;DR: Flexible nanogels with different degrees of flexibility based on dendritic polyglycerol sulfate to mimic cellular HS can multivalently interact with viral glycoproteins, shield virus surfaces, and efficiently block infection.
Journal ArticleDOI

Equine Herpesvirus 1 Enters Cells by Two Different Pathways, and Infection Requires the Activation of the Cellular Kinase ROCK1

TL;DR: It is shown that EHV-1 can enter disparate cell types by at least two distinct mechanisms and that productive infection is dependent upon the activation of ROCK1, and that activation of the serine/threonine Rho kinase ROCK1 is critical for infection.
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Size-dependent inhibition of herpesvirus cellular entry by polyvalent nanoarchitectures

TL;DR: It turned out that the derivatives inhibited virus infection at an early stage during entry but did not affect cell-to-cell spread, and tunable polyvalent nanomaterials are promising and efficient virus entry inhibitors, which can likely be used for a broad spectrum of enveloped viruses.
References
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Book

Molecular Cloning: A Laboratory Manual

TL;DR: Molecular Cloning has served as the foundation of technical expertise in labs worldwide for 30 years as mentioned in this paper and has been so popular, or so influential, that no other manual has been more widely used and influential.
Journal ArticleDOI

Initial interaction of herpes simplex virus with cells is binding to heparan sulfate.

TL;DR: It is shown that cell surface heparan sulfate serves as the initial receptor for both serotypes of herpes simplex virus (HSV), and that virions could bind to heparin, a related glycosaminoglycan, and that hepar in blocked virus adsorption.
Journal ArticleDOI

The DNA sequence of equine herpesvirus-1.

TL;DR: The complete DNA sequence was determined of a pathogenic British isolate of equine herpesvirus-1, a respiratory virus which can cause abortion and neurological disease, and comparisons of predicted amino acid sequences allowed the functions of many equine Herpesvirus 1 proteins to be assigned.
Journal ArticleDOI

Glycoprotein C of herpes simplex virus type 1 plays a principal role in the adsorption of virus to cells and in infectivity.

TL;DR: Although gC is dispensable for replication of herpes simplex virus in cell culture, it clearly facilitates virion adsorption and enhances infectivity by about a factor of 10.
Journal ArticleDOI

Glycoprotein C-independent binding of herpes simplex virus to cells requires cell surface heparan sulphate and glycoprotein B

TL;DR: The purpose of the studies reported here was to explore the requirements for infectivity of gC-negative HSV-1 mutants and found that absence or alteration of cell surface heparan sulphate significantly reduced the binding of g C-negative mutant virus and rendered cells resistant to infection, as shown previously for the wild-type virus.
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