Volume 10, Issue 1 (2019)
JMBS 2019, 10(1): 15-21 |
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Takrim S, Motamedi M, Jafari M, Amani J, Salmanian A. Expression, Purification and Immunogenicity Evaluation of Recombinant Fusion Protein (F) from Newcastle Virus in Animal Model. JMBS 2019; 10 (1) :15-21
URL: http://biot.modares.ac.ir/article-22-14018-en.html
URL: http://biot.modares.ac.ir/article-22-14018-en.html
1- National Institute of Genetic Engineering & Biotechnology (NIGEB), Tehran, Iran
2- Applied Microbiology Research Center, Baqiyatallah University of Medical Sciences, Tehran, Iran
3- National Institute of Genetic Engineering & Biotechnology (NIGEB), Tehran, Iran, Institute of Genetic Engineering & Biotechnology, Pajoohesh Boulevard, Shahrak-e Pajoohesh, 15 Kilometer Tehran-Karaj Highway, Tehran, Iran, Postal Code: 1497716316 , salman@nigeb.ac.ir
2- Applied Microbiology Research Center, Baqiyatallah University of Medical Sciences, Tehran, Iran
3- National Institute of Genetic Engineering & Biotechnology (NIGEB), Tehran, Iran, Institute of Genetic Engineering & Biotechnology, Pajoohesh Boulevard, Shahrak-e Pajoohesh, 15 Kilometer Tehran-Karaj Highway, Tehran, Iran, Postal Code: 1497716316 , salman@nigeb.ac.ir
Abstract: (9892 Views)
Newcastle disease virus (NDV) is an infectious agent of a large variety of birds, including chickens, which poses a real threat to the poultry industry. This virus is a member of the avian Paramyxoviridae. NDV is enveloped with membrane-embedded spikes consisting of glycosylated hemagglutinin (HN) and fusion (F) proteins. The mean death time after vNDV infection is 2-6 days, hence, the presence of preexisting antibodies prior to infection appears to be the most critical protection from this disease. Antibodies produced against the HN and F trans-membrane surface glycoproteins are able to neutralize NDV upon subsequent infection and inhibition of viral fusion with the host cell membrane, respectively. In this experimental study, the immunogenic epitopes of the F protein of NDV were designed artificially and were expressed in the heterologous system (Escherichia coli), using the appropriate vector (pET32a). In order to evaluate the immunogenicity of the recombinant f fragment, the protein was injected into the animal model. Immune response and the rise of specific antibodies titers were determined in immune sera. The results showed that immunization of mice with this recombinant protein could elicit significant serum IgG antibody up to 1/204800 titer. We show that the recombinant F protein was recognized by the mice sera immunized with the commercial vaccine. Moreover, the reactivity of vaccine strain virus with sera from F protein immunized mice suggested that the F protein is able to present similar epitopes with viral vaccine strain and hopefully could stimulate the immune system of the animal against the infectious viruses.
Article Type: Research Paper |
Subject:
Agricultural Biotechnology
Received: 2016/11/14 | Accepted: 2017/06/13 | Published: 2019/03/16
Received: 2016/11/14 | Accepted: 2017/06/13 | Published: 2019/03/16
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