scholarly journals Structure–function relationship in the ‘termination upstream ribosomal binding site’ of the calicivirus rabbit hemorrhagic disease virus

2019 ◽  
Vol 47 (4) ◽  
pp. 1920-1934
Author(s):  
René Wennesz ◽  
Christine Luttermann ◽  
Felix Kreher ◽  
Gregor Meyers
Keyword(s):  
Structure Function ◽  
Binding Site ◽  
Disease Virus ◽  
Rabbit Hemorrhagic Disease Virus ◽  
Hemorrhagic Disease ◽  
Rabbit Hemorrhagic Disease ◽  
Structure Function Relationship ◽  
Function Relationship ◽  
Ribosomal Binding Site

scholarly journals Structural Analysis of a Rabbit Hemorrhagic Disease Virus Binding to Histo-Blood Group Antigens

2014 ◽  
Vol 89 (4) ◽  
pp. 2378-2387 ◽  
Author(s):  
Mila M. Leuthold ◽  
Kevin P. Dalton ◽  
Grant S. Hansman
Keyword(s):  
Binding Site ◽  
Disease Virus ◽  
Rabbit Hemorrhagic Disease Virus ◽  
Hemorrhagic Disease ◽  
Blood Group Antigens ◽  
Content Type ◽  
Rabbit Hemorrhagic Disease ◽  
X Ray ◽  
X Ray Crystallography ◽  
P Domain

ABSTRACTRabbit hemorrhagic disease virus (RHDV) is a member of theCaliciviridaefamily (Lagovirusgenus). RHDV is highly contagious and attaches to epithelial cells in the digestive or respiratory tract, leading to massive lesions with high mortality rates. A new variant of RHDV (termed RHDVb) recently has emerged, and previously vaccinated rabbits appear to have little protection against this new strain. Similar to human norovirus (Caliciviridae,Norovirusgenus), RHDV binds histo-blood group antigens (HBGAs), and this is thought to be important for infection. Here, we report the HBGA binding site on the RHDVb capsid-protruding domain (P domain) using X-ray crystallography. The HBGA binding pocket was located in a negatively charged patch on the side of the P domain and at a dimeric interface. Residues from both monomers contributed to the HBGA binding and involved a network of direct hydrogen bonds and water-mediated interactions. An amino acid sequence alignment of different RHDV strains indicated that the residues directly interacting with the ABH-fucose of the HBGAs (Asp472, Asn474, and Ser479) were highly conserved. This result suggested that different RHDV strains also could bind HBGAs at the equivalent pocket. Moreover, several HBGA binding characteristics between RHDVb and human genogroup II norovirus were similar, which indicated a possible convergent evolution of HBGA binding interactions. Further structural studies with other RHDV strains are needed in order to better understand the HBGA binding mechanisms among the diverse RHDV strains.IMPORTANCEWe identified, for the first time, the HBGA binding site on an RHDVb P domain using X-ray crystallography. Our results showed that RHDVb and human genogroup II noroviruses had similar HBGA binding interactions. Recently, it was discovered that synthetic HBGAs or HBGA-expressing enteric bacteria could enhance human genogroup II norovirus infection in B cells. Considering that RHDVb and genogroup II norovirus similarly interacted with HBGAs, it may be possible that a comparable cell culture system also could work with RHDVb. Taken together, these new findings will extend our understanding of calicivirus HBGA interactions and may help to elucidate the specific roles of HBGAs in calicivirus infections.

scholarly journals A Review on the Methods Used for the Detection and Diagnosis of Rabbit Hemorrhagic Disease Virus (RHDV)

2021 ◽  
Vol 9 (5) ◽  
pp. 972
Author(s):  
Joana Abrantes ◽  
Ana M. Lopes
Keyword(s):  
Disease Virus ◽  
Diagnostic Tests ◽  
High Throughput Sequencing ◽  
Current Knowledge ◽  
European Rabbit ◽  
Rabbit Hemorrhagic Disease Virus ◽  
Hemorrhagic Disease ◽  
Rabbit Hemorrhagic Disease ◽  
Detection And Diagnosis

Since the early 1980s, the European rabbit (Oryctolagus cuniculus) has been threatened by the rabbit hemorrhagic disease (RHD). The disease is caused by a lagovirus of the family Caliciviridae, the rabbit hemorrhagic disease virus (RHDV). The need for detection, identification and further characterization of RHDV led to the development of several diagnostic tests. Owing to the lack of an appropriate cell culture system for in vitro propagation of the virus, much of the methods involved in these tests contributed to our current knowledge on RHD and RHDV and to the development of vaccines to contain the disease. Here, we provide a comprehensive review of the RHDV diagnostic tests used since the first RHD outbreak and that include molecular, histological and serological techniques, ranging from simpler tests initially used, such as the hemagglutination test, to the more recent and sophisticated high-throughput sequencing, along with an overview of their potential and their limitations.

A new variant of rabbit hemorrhagic disease virus G2-like strain isolated in China

2016 ◽  
Vol 215 ◽  
pp. 20-24 ◽  
Author(s):  
Bo Hu ◽  
Zhiyu Fan ◽  
Fang Wang ◽  
Yanhua Song ◽  
Houjun Wei ◽  
...  
Keyword(s):  
Disease Virus ◽  
Rabbit Hemorrhagic Disease Virus ◽  
Hemorrhagic Disease ◽  
Rabbit Hemorrhagic Disease ◽  
New Variant

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 Protection of Rabbits against Rabbit Hemorrhagic Disease Virus by Immunization with the VP60 Protein Expressed in Plants with a Potyvirus-Based Vector

Virology ◽  
2001 ◽  
Vol 280 (2) ◽  
pp. 283-291 ◽  
Author(s):  
María Rosario Fernández-Fernández ◽  
Mercedes Mouriño ◽  
José Rivera ◽  
Francisco Rodríguez ◽  
Juan Plana-Durán ◽  
...  
Keyword(s):  
Disease Virus ◽  
Rabbit Hemorrhagic Disease Virus ◽  
Hemorrhagic Disease ◽  
Rabbit Hemorrhagic Disease
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