Phosphoprotein Contributes to the Thermostability of Newcastle Disease Virus
Newcastle disease (ND), caused by Newcastle disease virus (NDV), is highly contagious and represents a major threat to the poultry industry. The thermostable vaccines are not insensitive to heat and ease of storage and transportation, but the mechanism of NDV thermostability remains unknown. The pho...
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doaj-11e9d6e97f5b4e5ab8a5e62275eb5e4c2020-11-25T00:05:06ZengHindawi LimitedBioMed Research International2314-61332314-61412018-01-01201810.1155/2018/89174768917476Phosphoprotein Contributes to the Thermostability of Newcastle Disease VirusYang Zhao0Huairan Liu1Feng Cong2Wei Wu3Ran Zhao4Xiangang Kong5College of Veterinary Medicine, Northeast Agricultural University, No. 600 Changjiang Street, Xiangfang District, Harbin 150030, Heilongjiang Province, ChinaDivision of Avian Infectious Diseases, National Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, The Chinese Academy of Agricultural Sciences, No. 678 Haping Road, Xiangfang District, Harbin 150069, ChinaDivision of Avian Infectious Diseases, National Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, The Chinese Academy of Agricultural Sciences, No. 678 Haping Road, Xiangfang District, Harbin 150069, ChinaDivision of Avian Infectious Diseases, National Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, The Chinese Academy of Agricultural Sciences, No. 678 Haping Road, Xiangfang District, Harbin 150069, ChinaDivision of Avian Infectious Diseases, National Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, The Chinese Academy of Agricultural Sciences, No. 678 Haping Road, Xiangfang District, Harbin 150069, ChinaCollege of Veterinary Medicine, Northeast Agricultural University, No. 600 Changjiang Street, Xiangfang District, Harbin 150030, Heilongjiang Province, ChinaNewcastle disease (ND), caused by Newcastle disease virus (NDV), is highly contagious and represents a major threat to the poultry industry. The thermostable vaccines are not insensitive to heat and ease of storage and transportation, but the mechanism of NDV thermostability remains unknown. The phosphoprotein (P), fusion protein (F), hemagglutinin-neuraminidase protein (HN), and large polymerase protein (L) are associated with NDV virulence. The association between F, HN, or L and viral thermostability has been, respectively, studied in different reports. However, the effects of P on NDV thermostability have not been demonstrated. Here, we utilized an existing reverse genetics system in our laboratory, to generate chimeric viruses by exchanging the P protein between the thermostable NDV4-C strain and the thermolabile LaSota strain. Chimeric viruses were found to possess similar growth properties, passage stability, and virulence, as compared to those of these parental strains. Interestingly, the thermostability of the chimera with P derived from the thermolabile LaSota strain was reduced compared to that of the parental virus, and P of the thermostable NDV4-C strain enhanced chimeric virus thermostability. Our data demonstrate that P is an important factor for the thermostability of NDV and provides information regarding the molecular mechanism of NDV thermostability; moreover, these results suggest a theoretical basis for using the NDV4-C strain as a thermostable vaccine.http://dx.doi.org/10.1155/2018/8917476 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Yang Zhao Huairan Liu Feng Cong Wei Wu Ran Zhao Xiangang Kong |
spellingShingle |
Yang Zhao Huairan Liu Feng Cong Wei Wu Ran Zhao Xiangang Kong Phosphoprotein Contributes to the Thermostability of Newcastle Disease Virus BioMed Research International |
author_facet |
Yang Zhao Huairan Liu Feng Cong Wei Wu Ran Zhao Xiangang Kong |
author_sort |
Yang Zhao |
title |
Phosphoprotein Contributes to the Thermostability of Newcastle Disease Virus |
title_short |
Phosphoprotein Contributes to the Thermostability of Newcastle Disease Virus |
title_full |
Phosphoprotein Contributes to the Thermostability of Newcastle Disease Virus |
title_fullStr |
Phosphoprotein Contributes to the Thermostability of Newcastle Disease Virus |
title_full_unstemmed |
Phosphoprotein Contributes to the Thermostability of Newcastle Disease Virus |
title_sort |
phosphoprotein contributes to the thermostability of newcastle disease virus |
publisher |
Hindawi Limited |
series |
BioMed Research International |
issn |
2314-6133 2314-6141 |
publishDate |
2018-01-01 |
description |
Newcastle disease (ND), caused by Newcastle disease virus (NDV), is highly contagious and represents a major threat to the poultry industry. The thermostable vaccines are not insensitive to heat and ease of storage and transportation, but the mechanism of NDV thermostability remains unknown. The phosphoprotein (P), fusion protein (F), hemagglutinin-neuraminidase protein (HN), and large polymerase protein (L) are associated with NDV virulence. The association between F, HN, or L and viral thermostability has been, respectively, studied in different reports. However, the effects of P on NDV thermostability have not been demonstrated. Here, we utilized an existing reverse genetics system in our laboratory, to generate chimeric viruses by exchanging the P protein between the thermostable NDV4-C strain and the thermolabile LaSota strain. Chimeric viruses were found to possess similar growth properties, passage stability, and virulence, as compared to those of these parental strains. Interestingly, the thermostability of the chimera with P derived from the thermolabile LaSota strain was reduced compared to that of the parental virus, and P of the thermostable NDV4-C strain enhanced chimeric virus thermostability. Our data demonstrate that P is an important factor for the thermostability of NDV and provides information regarding the molecular mechanism of NDV thermostability; moreover, these results suggest a theoretical basis for using the NDV4-C strain as a thermostable vaccine. |
url |
http://dx.doi.org/10.1155/2018/8917476 |
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