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Hemagglutinin–neuraminidase (HN) protein besides its mediation in viral pathogenesis, is composed of various antigenic sites which stimulate production of host’s antibodies. Thus, application of this protein in serological tests and vaccination plays a major role in biosecurity and control programs. In the present study, we designed a recombinant HN protein containing different neutralizing antigenic sites with velogenic patterns, and sub-cloned it into pET-43.1a+ expression vector. The expression of NusA-HN recombinant protein was induced. Affinity chromatography protein purification using HisPur? Ni–NTA was then conducted. Moreover, we performed western-blot technique using HRP-conjugated Anti His-Tag. Results revealed that following induction of recombinant protein, two distinct bands of HN-61 kDa and NusA-63 kDa were purified and identified by western-blotting. We recommend further analysis should be carried out to determine the functional role of this recombinant protein in enzyme-linked immunosorbent assays for Newcastle disease diagnosis. This HN protein containing multi neutralizing antigenic sites might also be applicable in vaccination programs to increase vaccines potency.  相似文献   
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International Journal of Peptide Research and Therapeutics - Fusion (F) and Hemagglutinin-neuraminidase (HN) glycoproteins of Newcastle disease virus containing important epitopes play crucial role...  相似文献   
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Molecular Biology Reports - Newcastle disease, is one of the most important diseases of the poultry industry, has many economic losses. The aim of this study was to isolate and determine the...  相似文献   
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