scholarly journals Minor structural protein VP2 in rabbit hemorrhagic disease virus downregulates the expression of the viral capsid protein VP60

2009 ◽  
Vol 90 (12) ◽  
pp. 2952-2955 ◽  
Author(s):  
Liu Chen ◽  
Guangqing Liu ◽  
Zheng Ni ◽  
Bin Yu ◽  
Tao Yun ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Disease Virus ◽  
Luciferase Assay ◽  
Rabbit Hemorrhagic Disease Virus ◽  
Hemorrhagic Disease ◽  
Mrna Levels ◽  
Structural Protein ◽  
Rabbit Hemorrhagic Disease ◽  
Minor Structural Protein ◽  
Capsid Protein Vp60

Rabbit hemorrhagic disease virus (RHDV) has two structural proteins: the major capsid protein VP60 and the minor capsid protein VP2. VP2 is speculated to play an important role in the virus life cycle. To investigate the effect of VP2 on VP60 expression, three types of experiment (baculovirus–insect cell system, mammalian–luciferase assay system and in vitro coupled transcription/translation system) were used to express VP60 alone or co-expressed with VP2. Both forms of VP60 were able to form virus-like particles in insect cells. Western blot analysis and dual-luciferase assays demonstrated that the presence of VP2 results in downregulation of the expression of VP60 in vivo. Real-time RT-PCR of mRNA levels showed that downregulation of VP60 occurs at the transcriptional level. The ability of the viral minor structural protein VP2 to regulate capsid protein levels may contribute to effective virus infection.

scholarly journals Recombinant Lactobacillus casei Expressing Capsid Protein VP60 can Serve as Vaccine Against Rabbit Hemorrhagic Disease Virus in Rabbits

Vaccines ◽  
2019 ◽  
Vol 7 (4) ◽  
pp. 172 ◽  
Author(s):  
Li Wang ◽  
Tian Xia ◽  
Tiantian Guo ◽  
Yi Ru ◽  
Yanping Jiang ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Disease Virus ◽  
Lactobacillus Casei ◽  
Rabbit Hemorrhagic Disease Virus ◽  
Economic Losses ◽  
High Morbidity ◽  
Hemorrhagic Disease ◽  
Rabbit Hemorrhagic Disease ◽  
Inactivated Vaccines ◽  
Capsid Protein Vp60

Rabbit hemorrhagic disease virus (RHDV) is the causative agent of rabbit hemorrhagic disease (RHD). RHD, characterized by hemorrhaging, liver necrosis, and high morbidity and mortality in rabbits and hares, causes severe economic losses in the rabbit industry worldwide. Due to the lack of an efficient in-vitro propagation system for RHDV, the current vaccine is produced via chemical inactivation of crude RHDV preparation derived from the livers of infected rabbits. Inactivated vaccines are effective for controlling RHD, but the potential problems of biosafety and animal welfare have negative effects on the application of inactivated vaccines. In this study, an oral Lactobacillus casei (L. casei) vaccine was used as an antigen delivery system to express RHDV capsid protein VP60(VP1)-eGFP fusion protein. The expression of the recombinant protein was confirmed via western blotting and immunofluorescence (IFA). Our results indicate that oral administration of this probiotic vaccine can stimulate secretory immunoglobulin A (SIgA)-based mucosal and IgG-based humoral immune responses in rabbits. The immunized rabbits were completely protected against challenge with RHDV. Our findings indicate that the L. casei expression system is a new strategy for the development of a safe and efficient vaccine against RHDV.

scholarly journals Immunization with Potato Plants Expressing VP60 Protein Protects against Rabbit Hemorrhagic Disease Virus

1999 ◽  
Vol 73 (5) ◽  
pp. 4452-4455 ◽  
Author(s):  
S. Castañón ◽  
M. S. Marín ◽  
J. M. Martín-Alonso ◽  
J. A. Boga ◽  
R. Casais ◽  
...  
Keyword(s):  
Disease Virus ◽  
Cauliflower Mosaic Virus ◽  
Rabbit Hemorrhagic Disease Virus ◽  
35S Promoter ◽  
Hemorrhagic Disease ◽  
Structural Protein ◽  
Transcriptional Enhancer ◽  
Leaf Extracts ◽  
Rabbit Hemorrhagic Disease ◽  
Potato Plants

ABSTRACT The major structural protein VP60 of rabbit hemorrhagic disease virus (RHDV) has been produced in transgenic potato plants under the control of a cauliflower mosaic virus 35S promoter or a modified 35S promoter that included two copies of a strong transcriptional enhancer. Both types of promoters allowed the production of specific mRNAs and detectable levels of recombinant VP60, which were higher for the constructs carrying the modified 35S promoter. Rabbits immunized with leaf extracts from plants carrying this modified 35S promoter showed high anti-VP60 antibody titers and were fully protected against the hemorrhagic disease.

scholarly journals Bioinformatics analysis of capsid protein of different subtypes rabbit hemorrhagic disease virus

2019 ◽  
Vol 15 (1) ◽  
Author(s):  
Ruibin Qi ◽  
Jie Zhu ◽  
Qiuhong Miao ◽  
Aoxing Tang ◽  
Dandan Dong ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Disease Virus ◽  
Genetic Relationship ◽  
Antigenic Variation ◽  
Rabbit Hemorrhagic Disease Virus ◽  
Hemorrhagic Disease ◽  
Phosphorylation Sites ◽  
Rabbit Hemorrhagic Disease ◽  
Glycosylation Sites ◽  
Viral Virulence

Abstract Background Rabbit Hemorrhagic Disease Virus (RHDV) belongs to the Caliciviridae family, is a highly lethal pathogen to rabbits. Increasing numbers of studies have demonstrated the existence of antigenic variation in RHDV, leading to the emergence of a new RHDV isolate (RHDVb). However, the underlying factors determining the emergence of the new RHDV and its unpredictable epidemiology remain unclear. To investigate these issues, we selected more than 184 partial and/or complete genome sequences of RHDV from GenBank and analyzed their phylogenetic relationships, divergence, and predicted protein modification sites. Results Phylogenetic analysis showed that classic RHDV isolates, RHDVa, and RHDVb formed different clades. It’s interesting to note that RHDVa being more closely related to classic RHDV than RHDVb, while RHDVb had a closer genetic relationship to Rabbit Calicivirus (RCV) than to classic RHDV isolates. Moreover, divergence analysis suggested that the accumulation of amino acid (aa) changes might be a consequence of adaptive diversification of capsid protein (VP60) during the division between classical RHDV, RHDVa, RHDVb, and RCV. Notably, the prediction of N-glycosylation sites suggested that RHDVb subtypes had two unique N-glycosylation sites (aa 301, 362) but lacked three other N-glycosylation sites (aa 45, 308, 474) displayed in classic RHDV and RHDVa VP60 implying this divergence of N-glycosylation sites in RHDV might affect viral virulence. Analysis of phosphorylation sites also indicated that some phosphorylation sites in RHDVa and RHDVb differed from those in classic RHDV, potentially related to antigenic variation in RHDV. Conclusion The genetic relationship between RHDVb and RCV was closer than classic RHDV isolates. Moreover, compared to RHDV and RHDVa, RHDVb had two unique N-glycosylation sites but lacked three sites, which might affect the virulence of RHDV. These results may provide new clues for further investigations of the origin of new types of RHDV and the mechanisms of genetic variation in RHDV.

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