scholarly journals Display of Classical Swine Fever Virus E2 Protein BC Antigenic Domain on the Cell Surface of Saccharomyces cerevisiae

2017 ◽  
Vol 06 (03) ◽  
pp. 72-78
Author(s):  
小凤 刘
2015 ◽  
Vol 81 (11) ◽  
pp. 3745-3752 ◽  
Author(s):  
Yi-Gang Xu ◽  
Xue-Ting Guan ◽  
Zhong-Mei Liu ◽  
Chang-Yong Tian ◽  
Li-Chun Cui

ABSTRACTClassical swine fever, caused by classical swine fever virus (CSFV), is a highly contagious disease that results in enormous economic losses in pig industries. The E2 protein is one of the main structural proteins of CSFV and is capable of inducing CSFV-neutralizing antibodies and cytotoxic T lymphocyte (CTL) activitiesin vivo. Thymosin α-1 (Tα1), an immune-modifier peptide, plays a very important role in the cellular immune response. In this study, genetically engineeredLactobacillus plantarumbacteria expressing CSFV E2 protein alone (L. plantarum/pYG-E2) and in combination with Tα1 (L. plantarum/pYG-E2-Tα1) were developed, and the immunogenicity of each as an oral vaccine to induce protective immunity against CSFV in pigs was evaluated. The results showed that recombinantL. plantarum/pYG-E2 andL. plantarum/pYG-E2-Tα1 were both able to effectively induce protective immune responses in pigs against CSFV infection by eliciting immunoglobulin A (IgA)-based mucosal, immunoglobulin G (IgG)-based humoral, and CTL-based cellular immune responses via oral vaccination. Significant differences (P< 0.05) in the levels of immune responses were observed betweenL. plantarum/pYG-E2-Tα1 andL. plantarum/pYG-E2, suggesting a better immunogenicity ofL. plantarum/pYG-E2-Tα1 as a result of the Tα1 molecular adjuvant that can enhance immune responsiveness and augment specific lymphocyte functions. Our data suggest that the recombinantLactobacillusmicroecological agent expressing CSFV E2 protein combined with Tα1 as an adjuvant provides a promising strategy for vaccine development against CSFV.


Vaccine ◽  
2016 ◽  
Vol 34 (33) ◽  
pp. 3723-3730 ◽  
Author(s):  
Xun Liao ◽  
Zuohuan Wang ◽  
Tong Cao ◽  
Chao Tong ◽  
Shichao Geng ◽  
...  

2014 ◽  
Vol 159 (12) ◽  
pp. 3219-3230 ◽  
Author(s):  
Myunghwan Jung ◽  
Yun Ji Shin ◽  
Ju Kim ◽  
Seung-Bin Cha ◽  
Won-Jung Lee ◽  
...  

2013 ◽  
Vol 113 (3) ◽  
pp. 483-490 ◽  
Author(s):  
Jinn-Chin Yiu ◽  
Cheng-Wei Liu ◽  
Ruei-Yuan Su ◽  
Wan-Jun Lai ◽  
Menq-Jiau Tseng ◽  
...  

2020 ◽  
Vol 167 ◽  
pp. 105527
Author(s):  
Ding Li ◽  
Junchen Wu ◽  
Jin Chen ◽  
Dong Zhang ◽  
Yuanpeng Zhang ◽  
...  

Viruses ◽  
2020 ◽  
Vol 12 (4) ◽  
pp. 388 ◽  
Author(s):  
Elizabeth A. Vuono ◽  
Elizabeth Ramirez-Medina ◽  
Keith Berggren ◽  
Ayushi Rai ◽  
Sarah Pruitt ◽  
...  

Interactions between the major structural glycoprotein E2 of classical swine fever virus (CSFV) with host proteins have been identified as important factors affecting virus replication and virulence. Previously, using the yeast two-hybrid system, we identified swine host proteins specifically interacting with CSFV E2. In this report, we use a proximity ligation assay to demonstrate that swine host protein CCDC115 interacts with E2 in CSFV-infected swine cells. Using a randomly mutated E2 library in the context of a yeast two-hybrid methodology, specific amino acid mutations in the CSFV E2 protein responsible for disrupting the interaction with CCDC115 were identified. A recombinant CSFV mutant (E2ΔCCDC115v) harboring amino acid changes disrupting the E2 protein interaction with CCDC115 was produced and used as a tool to assess the role of the E2–CCDC115 interaction in viral replication and virulence in swine. CSFV E2ΔCCDC115v showed a slightly decreased ability to replicate in the SK6 swine cell line and a greater replication defect in primary swine macrophage cultures. A decreased E2–CCDC115 interaction detected by PLA is observed in cells infected with E2ΔCCDC115v. Importantly, animals intranasally infected with 105 TCID50 of E2ΔCCDC115v experienced a significantly longer survival period when compared with those infected with the parental Brescia strain. This result would indicate that the ability of CSFV E2 to bind host CCDC115 protein during infection plays an important role in virus replication in swine macrophages and in virus virulence during the infection in domestic swine.


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