Mapping the membrane proteins of Newcastle-disease virus with a photoreactive glycolipid probe.
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ABSTRACT:
SUBMITTER: Bramhall JS
PROVIDER: S-EPMC1186431 | biostudies-other | 1979 Feb
REPOSITORIES: biostudies-other
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Project description:The newly emerged Duck Tembusu virus (DTMUV) is responsible for considerable economic loss in waterfowl-raising areas in China since 2010. Meanwhile, the virulent Newcastle disease virus (NDV) has also caused sporadic outbreaks in waterfowl. The individual vaccines against both diseases are available, however, there is no bivalent or combined vaccine for either disease. Here, we constructed a recombinant NDV-vectored vaccine candidate that expresses the pre-membrane (prM) and envelope (E) genes from DTMUV, designated as aGM/prM + E. The foreign prM and E proteins were stably expressed in aGM/prM + E and exhibited similar pathogenicity but higher growth kinetics than those of the parental virus. The aGM/prM + E carries a fusion cleavage site in accordance with avirulent viruses that have been frequently isolated from waterfowl, and induced remarkably (p < 0.001) higher NDV-specific hemagglutination inhibition (HI) titers than commercially available live NDV vaccines (LaSota strain). The aGM/prM + E also elicited significantly higher (p < 0.05) virus neutralization (VN) titers than commercially available DTMUV inactivated vaccines (HB strain). The aGM/prM + E not only provided complete protection against NDV challenge but also reduced the gross lesions on ovarian folliculi and provided 80% protection against DTMUV in ducks. We note that the aGM/prM + E vaccine can prevent challenged ducks from shedding of NDV and DTMUV. Our results suggest that the candidate vaccine aGM/prM + E would help decrease NDV and DTMUV transmissions in waterfowl raising areas in China.
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Project description:Newcastle disease virus is a member of family Paramyxoviridae that infects chicken. Its genome comprises ~15.2 kb negative-sense RNA that encodes six major proteins. The virus encodes various proteins; among all, nucleocapsid (NP) and matrix (M) help in virus replication and its budding from the host cells, respectively. In this study, we investigated the intracellular distribution of NP and M upon expression in the yeast Saccharomyces cerevisiae. We observed nuclear targeting of M, and vacuolar localization of NP was observed in a fraction of yeast cells. Prolonged expression of GFP fused NP or M resulted in altered cell viability and intracellular production of reactive oxygen species in yeast cells. The expression of viral proteins did not alter the morphology and number of the organelles such as nucleus, mitochondria, endoplasmic reticulum, and peroxisomes. However, a significant effect was observed on vacuolar morphology and number in yeast cells. These observations point towards the importance of host cellular reorganization in viral infection. These findings may enable us to understand the conserved pathways affected in eukaryotic cells as a result of viral protein expression.Supplementary informationThe online version contains supplementary material available at 10.1007/s13205-020-02624-4.
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Project description:We report the genetic plasticity of Newcastle disease virus. We introduced insertional mutation in the virus genome and checked fitness by comparing distribution of mutants in passage 1 and passage 2.
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Project description:The fusion (F) and haemagglutinin-neuraminidase (HN) proteins of Newcastle disease virus (NDV) are multifunctional proteins that play critical roles during infection. Here, we assessed the ability of NDV to replicate in macrophages and investigated the contribution of the F and HN proteins to NDV infection/replication in these cells. Results of our study revealed that, while presenting similar replication kinetics in a fibroblast cell line (DF1) or in primary non-adherent splenocytes, the NDV strain CA02 replicates better in macrophages (HD11 and primary adherent splenocytes) than the NDV strain Anhinga/93. Notably, exchange of the HN or both F and HN genes of NDV Anhinga/93 by the corresponding genes from NDV CA02 markedly improved the ability of the chimeric viruses to replicate in macrophages. These results indicate that the F and HN proteins are determinants of NDV macrophage host range. This represents the first description of productive NDV infection in macrophages.
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Project description:Newcastle disease virus (NDV) strain F is a lentogenic vaccine strain used for primary vaccination in day-old chickens against Newcastle disease (ND) in India and Southeast Asian countries. Recombinant NDV-F virus and another recombinant NDV harboring the major capsid protein VP2 gene of a very virulent infectious bursal disease virus (IBDV); namely rNDV-F and rNDV-F/VP2, respectively, were generated using the NDV F strain. The rNDV-F/VP2 virus was slightly attenuated, as compared to the rNDV-F virus, as evidenced from the mean death time and intracerebral pathogenicity index analysis. This result indicates that rNDV-F/VP2 behaves as a lentogenic virus and it is stable even after 10 serial passages in embryonated chicken eggs. When chickens were vaccinated with the rNDV F/VP2, it induced both humoral and cell mediated immunity, and was able to confer complete protection against very virulent IBDV challenge and 80% protection against virulent NDV challenge. These results suggest that rNDV-F could be an effective and inherently safe vaccine vector. Here, we demonstrate that a bivalent NDV-IBDV vaccine candidate generated by reverse genetics method is safe, efficacious and cost-effective, which will greatly aid the poultry industry in developing countries.
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Project description:BACKGROUND:Sensitive and specific antibodies can be used as essential probes to develop competitive enzyme-linked immunosorbent assay (cELISA). However, traditional antibodies are difficult to produce, only available in limited quantities, and ineffective as enzymatic labels. Nanobodies, which are single-domain antibodies (sdAbs), offer an alternative, more promising tool to circumvent these limitations. In the present work, a cELISA using nanobody-horseradish peroxidase (HRP) fusion protein firstly designed as a probe was developed for detecting anti-Newcastle disease virus (NDV) antibodies in chicken sera. RESULTS:In the study, a platform for the rapid and simple production of nanobody-HRP fusion protein was constructed. First, a total of 9 anti-NDV-NP protein nanobodies were screened from a immunised Bactrian camel. Then, the Nb5-HRP fusions were produced with the platform and used for the first time as sensitive reagents for developing cELISA to detect anti-NDV antibodies. The cut-off value of the cELISA was 18%, and the sensitivity and specificity were respectively 100% and 98.6%. The HI test and commercial ELISA kit (IDEXX) separately agreed 97.83% and 98.1% with cELISA when testing clinical chicken sera and both agreed 100% when testing egg yolks. However, for detecting anti-NDV antibodies in the sequential sera from the challenged chickens, cELISA demonstrated to be more sensitive than the HI test and commercial ELISA kit. Moreover, a close correlation (R2?=?0.914) was found between the percent competitive inhibition values of cELISA and HI titers. CONCLUSIONS:A platform was successfully designed to easily and rapidly produce the nanobody-HRP fusion protein, which was the first time to be used as reagents for establishing cELISA. Results suggest that the platform supports the development of a cELISA with high sensitivity, simplicity, and rapid detection of anti-NDV antibodies. Overall, we believe that the platform based on nanobody-HRP fusions can be widely used for future investigations and treatment other diseases and viruses.
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