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полный	информационный	краткий

Поисковый запрос: (<.>S=GENETIC-ANALYSIS<.>)

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Study of the immunogenicity of the VP2 protein of canine parvovirus produced using an improved Baculovirus expression system / D. Chang, Y. K. Liu, Y. Y. Chen [et al.] // BMC Vet. Res. - 2020. - Vol. 16, Is. 1. - Ст. 202, DOI 10.1186/s12917-020-02422-3. - Cited References:30. - This work was financially supported by the National Natural Science Foundation of China (No. 31870917), The program for Innovative Research Team of Science and Technology in University of Henan Province (No. 20IRTSTHN024) and Key Scientific Research Projects of Colleges and Universities in Henan Province of China (No. 18B230008). The funding bodies played no role in the design of the study, the collection, analysis, and interpretation of data and in writing the manuscript. . - ISSN 1746-6148

РУБ Veterinary Sciences
Рубрики:
VIRUS-LIKE PARTICLES
   ESCHERICHIA-COLI
   GENETIC-ANALYSIS
   CPV-VP2
Кл.слова (ненормированные):
Canine parvovirus -- VP2 protein -- Baculovirus expression system
Аннотация: Background Canine parvovirus (CPV) is now recognized as a serious threat to the dog breeding industry worldwide. Currently used CPV vaccines all have their specific drawbacks, prompting a search for alternative safe and effective vaccination strategies such as subunit vaccine. VP2 protein is the major antigen targeted for developing CPV subunit vaccine, however, its production in baculovirus expression system remains challenging due to the insufficient yield. Therefore, our study aims to increase the VP2 protein production by using an improved baculovirus expression system and to evaluate the immunogenicity of the purified VP2 protein in mice. Results The results showed that high-level expression of the full length VP2 protein was achieved using our modified baculovirus expression system. The recombinant virus carrying two copies of VP2 gene showed the highest expression level, with a productivity of 186 mg/L, which is about 1.4-1.6 fold that of the recombinant viruses carrying only one copy. The purified protein reacted with Mouse anti-His tag monoclonal antibody and Rabbit anti-VP2 polyclonal antibody. BALB/c mice were intramuscularly immunized with purified VP2 protein twice at 2 week intervals. After vaccination, VP2 protein could induce the mice produce high level of hemagglutination inhibition antibodies. Conclusions Full length CPV VP2 protein was expressed at high level and purified efficiently. Moreover, it stimulated mice to produce high level of antibodies with hemmaglutination inhibition properties. The VP2 protein expressed in this study could be used as a putative economic and efficient subunit vaccine against CPV infection.

WOS
Держатели документа:
Nanyang Normal Univ, Sch Agr Engn, Henan Provincal Engn & Technol Ctr Hlth Prod Live, Nanyang 473061, Peoples R China.
Nanyang Normal Univ, Sch Agr Engn, Key Lab Ecol Secur, Nanyang 473061, Peoples R China.
Nanyang Normal Univ, Sch Agr Engn, Collaborat Innovat Ctr Water Secur Water Source R, Nanyang 473061, Peoples R China.
Russian Acad Sci, Fed Res Ctr, Krasnoyarsk Sci Ctr, Inst Biophys,Siberian Branch, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Chang, Dao; Liu, Yangkun; Chen, Yangyang; Hu, Xiaomin; Burov, Andrey; Puzyr, Alexey; Bondar, Vladimir; Yao, Lunguang; National Natural Science Foundation of ChinaNational Natural Science Foundation of China [31870917]; program for Innovative Research Team of Science and Technology in University of Henan Province [20IRTSTHN024]; Key Scientific Research Projects of Colleges and Universities in Henan Province of China [18B230008]

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