Resistance to pseudorabies virus infection in transformed cell lines expressing a soluble form of porcine herpesvirus entry mediator C.
Porcine herpesvirus entry mediator C (HveC) is an alphaherpesvirus receptor that binds to virion glycoprotein D (gD). Porcine HveC mediates entry of pseudorabies virus (PRV), herpes simplex virus types 1 and 2 (HSV-1 and HSV-2) and bovine herpesvirus type 1 (BHV-1). In order to assess the antiviral potential of a soluble form of porcine HveC, Vero cells were transformed with the chimeric gene expressing a fusion protein (PHveCIg) consisting of an extracellular domain of porcine HveC and the Fc portion of human IgG1. The transformed cell lines expressing PHveCIg showed marked resistance to PRV infection. Resistance to infection by other alphaherpesviruses (HSV-1 and BHV-1) was also observed in the transformed cell line. The present results demonstrate that a soluble form of porcine HveC is able to exert a significant antiviral effect against pseudorabies virus and other alphaherpesvirus infection in vitro.
Ono
Etsuro
E
Laboratory of Animal Experiment for Disease Model, Institute for Genetic Medicine, Hokkaido University, Sapporo 060-0815, Japan.
Amagai
Keiko
K
Sankyo Labo Service Corporation, Tokyo 132-0023, Japan.|Laboratory of Animal Experiment for Disease Model, Institute for Genetic Medicine, Hokkaido University, Sapporo 060-0815, Japan.
Yoshino
Saori
S
Gene Techno Science, Sapporo 062-8517, Japan.|Laboratory of Animal Experiment for Disease Model, Institute for Genetic Medicine, Hokkaido University, Sapporo 060-0815, Japan.
Taharaguchi
Satoshi
S
Laboratory of Animal Experiment for Disease Model, Institute for Genetic Medicine, Hokkaido University, Sapporo 060-0815, Japan.
Inobe
Manabu
M
Division of Molecular Immunology, Research Section of Molecular Pathogenesis, Institute for Genetic Medicine, Hokkaido University, Sapporo 060-0815, Japan.
Uede
Toshimitsu
T
Division of Molecular Immunology, Research Section of Molecular Pathogenesis, Institute for Genetic Medicine, Hokkaido University, Sapporo 060-0815, Japan.
D000818:Animals; D002417:Cattle; D002460:Cell Line; D002461:Cell Line, Transformed; D002522:Chlorocebus aethiops; D007242:Herpesvirus 1, Bovine / Q000472:pathogenicity; D018259:Herpesvirus 1, Human / Q000472:pathogenicity; D011558:Herpesvirus 1, Suid / Q000187:drug effects / Q000472:pathogenicity*; D049673:History, 20th Century; D007141:Immunoglobulin Fc Fragments / Q000235:genetics / Q000276:immunology / Q000378:metabolism; D007074:Immunoglobulin G / Q000737:chemistry; D011557:Pseudorabies / Q000517:prevention & control*; D018124:Receptors, Tumor Necrosis Factor / Q000235:genetics / Q000378:metabolism*; D053240:Receptors, Tumor Necrosis Factor, Member 14; D011991:Receptors, Virus / Q000235:genetics / Q000378:metabolism*; D012995:Solubility; D013552:Swine; D014709:Vero Cells; D010948:Viral Plaque Assay
D007141:Immunoglobulin Fc Fragments; D007074:Immunoglobulin G; D018124:Receptors, Tumor Necrosis Factor; D053240:Receptors, Tumor Necrosis Factor, Member 14; D011991:Receptors, Virus; C506028:TNFRSF14 protein, human