In this study ,IBV HH06 complete E gene was firstly cloned and sequenced .According to the hydrophilicity and antigenic index analysis ,its partial gene (193 to 327 bp) was subcloned into prokaryotic expression vector pET‐32a(+ ) and eukaryotic expression vector PVAX1 .The recombinant plasmid pET‐32a‐E1 was transformed into E .coli Rosetta (DE3) and induced with IPTG .The recombinant IBV truncated E1 protein with molecular weight of 23 ku was observed as expected .It could be recognized by positive IBV antisera in Western blotting with high reactivity . Then the purified recombinant protein was used as antigen for immunization of rabbit to prepare polyclonal antibody .Indirect ELISA showed that the titer of polyclonal antibody was 220 ,and it had high reactivity and specialty with recombinant protein .Furthermore ,IFA test demonstrated that this polyclonal antibody could react with Hela cells transfected with PVAX‐E1 plasmid and IBV‐infected CEK cells .T he IBV E polyclonal antibody obtained in this study laid a foundation for further functional research of E protein in IBV pathogenesis .%采用RT‐PCR方法扩增鸡传染性支气管炎病毒（infectious bronchitis virus ，IBV）HH06株 E基因全长，经抗原性和亲水性分析，将 E基因部分序列（193～327 bp）亚克隆于pET‐32a（＋）和PVAX1载体中。将阳性重组质粒pET‐32a‐E1转化 E.coli Rosetta （DE3）感受态细胞，诱导表达获得大小约为23 ku的重组截短E1蛋白，Western blotting检测重组蛋白与IBV全病毒多克隆抗体能特异性反应。以纯化后的E1蛋白免疫新西兰白兔制备多克隆抗体，ELISA检测抗体效价达到220；Western blotting 分析表明，E1多克隆抗体与重组表达蛋白具有良好的反应性；间接免疫荧光试验显示，多克隆抗体可检测到 PVAX‐E1转染 Hela细胞表达的 E1蛋白和感染鸡胚肾细胞（CEK ）中的 H H06株IBV ，抗E蛋白多克隆抗体的制备为E蛋白功能的深入研究奠定了基础。
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