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Comparison of the antiviral potentials among the pseudorabies-resistant transgenes encoding different soluble forms of porcine nectin-1 in transgenic mice

¹ Laboratory of Biomedicine, Center of Biomedical Research, Graduate School of Medical Sciences, Kyushu University, Fukuoka 812-8582, Japan
² The Avian Zoonoses Research Center, Faculty of Agriculture, Tottori University, Tottori 680-8553, Japan
³ Laboratory of Animal Experiment for Disease Model, Institute for Genetic Medicine, Hokkaido University, Sapporo 060-0815, Japan
⁴ Sankyo Labo Service Corporation, Tokyo 132-0023, Japan
⁵ France Hybrides, Saint-Jean-de-Braye, France

Correspondence
Etsuro Ono
etsuro{at}qda.med.kyushu-u.ac.jp

Nectin-1 is an alphaherpesvirus receptor that binds to virion glycoprotein D by the first immunoglobulin (Ig)-like domain. The possibility of making animals resistant to pseudorabies virus (PRV) infection has been investigated by generating transgenic mice expressing soluble forms of porcine nectin-1. Previously, transgenic mice were generated that expressed a fusion protein made of the entire ectodomain of nectin-1 fused to the Fc portion of human IgG, or the first Ig-like domain fused to the Fc portion of porcine IgG. Here, the contribution of the second and third Ig-like domains of nectin-1 was analysed by generating transgenic mice expressing the entire ectodomain of nectin-1 fused to the porcine Fc portion. Transgenic mice expressing each of three different fusion proteins were challenged with PRV for comparison of their resistance. Altogether, mice transgenic for a chimera that carried the entire ectodomain were more resistant than those transgenic for a chimera that carried the first Ig-like domain.