Baculovirus-mediated delivery of viral hemorrhagic septicemia virus G protein in forms of envelope-spiked protein and a CMV promoter-driven expression cassette

Aquaculture ◽  
2021 ◽  
pp. 737426
Author(s):  
Jeong In Yang ◽  
Ki Hong Kim
1998 ◽  
Vol 72 (12) ◽  
pp. 10189-10196 ◽  
Author(s):  
Katja Einer-Jensen ◽  
Thomas N. Krogh ◽  
Peter Roepstorff ◽  
Niels Lorenzen

ABSTRACT Viral hemorrhagic septicemia virus (VHSV) infections cause high losses in cultured rainbow trout in Europe. Attempts to produce a recombinant vaccine based on the transmembrane glycoprotein (G protein) have indicated that proper folding is important for the antigenicity and immunogenicity of the protein. The present study was initiated to identify the disulfide bonds and other structural aspects relevant to vaccine design. The N-terminal amino acid residue was identified as being a pyroglutamic acid, corresponding to Gln21 of the primary transcript. Peptides from endoproteinase-degraded G protein were analyzed by mass spectrometry before and after chemical reduction, and six disulfide bonds were identified: Cys29-Cys339, Cys44-Cys295, Cys90-Cys132, Cys172-Cys177, Cys195-Cys265, and Cys231-Cys236. Mass spectrometric analysis in combination with glycosidases allowed characterization of the glycan structure of the G protein. Three of four predicted N-linked oligosaccharides were found to be predominantly biantennary complex-type structures. Furthermore, an O-linked glycan near the N terminus was identified. Alignment of the VHSV G protein with five other rhabdovirus G proteins indicates that eight cysteine residues are situated at conserved positions. This finding suggests that there might be some common disulfide bonding pattern among the six rhabdoviruses.


2017 ◽  
Vol 126 (3) ◽  
pp. 211-227 ◽  
Author(s):  
RG Getchell ◽  
ER Cornwell ◽  
S Bogdanowicz ◽  
J Andrés ◽  
WN Batts ◽  
...  

Viruses ◽  
2020 ◽  
Vol 13 (1) ◽  
pp. 28
Author(s):  
So-Ri Han ◽  
Hetron M. Munang’andu ◽  
In-Kyu Yeo ◽  
Sung-Hyun Kim

Viral hemorrhagic septicemia virus (VHSV) is a highly pathogenic virus that infects a wide range of host fish species causing high economic losses in aquaculture. Epithelial cells in mucosal organs are target sites for VHSV entry into fish. To protect fish against VHSV infection, there is a need to develop antiviral compounds able to prevent establishment of infection at portals of virus entry into fish. Bacillus subtilis is a probiotic with excellent antiviral properties, of which one of its secretions, surfactin, has been shown to inhibit viral infections in mammals. Herein, we demonstrate its ability to prevent VHSV infection in olive flounder (Paralichthys olivaceus) intestinal epithelial cells (IECs) and infection in internal organs. Our findings show inhibition of VHSV infection in IECs by B. subtilis and surfactin. In addition, our findings showed inhibition of VHSV in Epithelioma Papulosum Cyprini (EPC) cells inoculated with intestinal homogenates from the fish pretreated with B. subtilis by oral exposure, while the untreated fish had cytopathic effects (CPE) caused by VHSV infection in the intestines at 48 h after the VHSV challenge. At 96 h post-challenge, samples from the untreated fish had CPE from head kidney and spleen homogenates and no CPE were observed in the intestinal homogenates, while the B. subtilis-pretreated fish had no CPE in all organs. These findings demonstrate that inhibition of VHSV infection at portals of virus entry in the intestines culminated in prevention of infection in internal organs. In summary, our results show that B. subtilis has the potential to prevent VHSV infection in fish and that its use as a probiotic in aquaculture has the potential to serve as an antiviral therapeutic agent against different viral infections.


2012 ◽  
Vol 43 (4) ◽  
pp. 459-476 ◽  
Author(s):  
Geoffrey H. Groocock ◽  
Stephen A. Frattini ◽  
Emily R. Cornwell ◽  
Laura L. Coffee ◽  
Gregory A. Wooster ◽  
...  

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