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Glycoproteins D of Equine Herpesvirus Type 1 (EHV-1) and EHV-4 Determine Cellular Tropism Independently of Integrins

https://doi.org/10.1128/jvi.06555-11
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Outgoing claims: the papers this work cites, builds on, or argues with.

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Identification and comparative sequence analysis of a gene in equine herpesvirus 1 with homology to the herpes simplex virus glycoprotein D gene
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Evidence for involvement of equine herpesvirus 1 glycoprotein B in cell-cell fusion
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Host cell tropism of equine herpesviruses: glycoprotein D of EHV-1 enables EHV-4 to infect a non-permissive cell line
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The order Herpesvirales
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Cloning of the genome of equine herpesvirus 4 strain TH20p as an infectious bacterial artificial chromosome
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EHV-1 glycoprotein D (EHV-1 gD) is required for virus entry and cell-cell fusion, and an EHV-1 gD deletion mutant induces a protective immune response in mice
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Glycoprotein C of equine herpesvirus 4 plays a role in viral binding to cell surface heparan sulfate
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Evidence for a differential functional regulation of the two β3-integrins αVβ3 and αIIbβ3
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The minimal essential sequence for a major cell type-specific adhesion site (CS1) within the alternatively spliced type III connecting segment domain of fibronectin is leucine-aspartic acid-valine
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A comparison of equid herpesvirus-1 (EHV-1) vascular lesions in the early versus late pregnant equine uterus
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Equine Herpesviruses 4 (Equine Rhinopneumonitis Virus) and 1 (Equine Abortion Virus)
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Integrin α3β1 (CD 49c/29) Is a Cellular Receptor for Kaposi's Sarcoma-Associated Herpesvirus (KSHV/HHV-8) Entry into the Target Cells
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Integrins
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Cloning of the Genomes of Equine Herpesvirus Type 1 (EHV‐1) Strains KyA and RacL11 as Bacterial Artificial Chromosomes (BAC)
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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
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Identification of the Integrin VLA-2 as a Receptor for Echovirus 1
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Entry of Alphaherpesviruses Mediated by Poliovirus Receptor-Related Protein 1 and Poliovirus Receptor
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New Perspectives in Cell Adhesion: RGD and Integrins
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Integrins and Signal Transduction Pathways: the Road Taken
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Equus caballus Major Histocompatibility Complex Class I Is an Entry Receptor for Equine Herpesvirus Type 1
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Equine Herpesvirus 1 Enters Cells by Two Different Pathways, and Infection Requires the Activation of the Cellular Kinase ROCK1
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Equine Herpesvirus 1 Entry via Endocytosis Is Facilitated by αV Integrins and an RSD Motif in Glycoprotein D
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Engineered Disulfide Bonds in Herpes Simplex Virus Type 1 gD Separate Receptor Binding from Fusion Initiation and Viral Entry
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Herpes Simplex Virus Glycoproteins H/L Bind to Cells Independently of αVβ3 Integrin and Inhibit Virus Entry, and Their Constitutive Expression Restricts Infection
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Structure-Based Mutagenesis of Herpes Simplex Virus Glycoprotein D Defines Three Critical Regions at the gD-HveA/HVEM Binding Interface
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Equine Herpesvirus 1 Utilizes a Novel Herpesvirus Entry Receptor
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Lack of Detectable Interaction between HSV-1 and Integrins or Tachykinins
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Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Equine Herpesviruses
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Equine Herpesvirus Type 4 UL56 and UL49.5 Proteins Downregulate Cell Surface Major Histocompatibility Complex Class I Expression Independently of Each Other
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