scholarly journals Evaluation of a subunit vaccine candidate (Biotech Vac Cox) against Eimeria spp. in broiler chickens

2021 ◽  
pp. 101329
Author(s):  
Emanuel Gumina ◽  
Jeffrey W. Hall ◽  
Bruno Vecchi ◽  
Xochitl Hernandez-Velasco ◽  
Brett Lumpkins ◽  
...  
2021 ◽  
Author(s):  
Jiahao Ma ◽  
Danmei Su ◽  
Yinyan Sun ◽  
Xueqin Huang ◽  
Ying Liang ◽  
...  

Within a year after its emergence, the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has infected over 100 million people worldwide with a death toll over 2 million. Vaccination remains the best hope to ultimately put this pandemic to an end. Here, using Trimer-Tag technology, we produced both wild-type (WT) and furin site mutant (MT) S-Trimers for COVID-19 vaccine studies. Cryo-EM structures of the WT and MT S-Trimers, determined at 3.2 Å and 2.6 Å respectively, revealed that both antigens adopt a tightly closed conformation and their structures are essentially identical to that of the previously solved full-length WT S protein in detergent. The tightly closed conformation is stabilized by fatty acid and polysorbate 80 binding at the receptor binding domains (RBDs) and the N terminal domains (NTDs) respectively. Additionally, we identified an important pH switch in the WT S-Trimer that shows dramatic conformational change and accounts for its increased stability at lower pH. These results validate Trimer-Tag as a platform technology in production of metastable WT S-Trimer as a candidate for COVID-19 subunit vaccine. IMPORTANCE Effective vaccine against SARS-CoV-2 is critical to end the COVID-19 pandemic. Here, using Trimer-Tag technology, we are able to produce stable and large quantities of WT S-Trimer, a subunit vaccine candidate for COVID-19 with high safety and efficacy from animal and Phase 1 clinical trial studies. Cryo-EM structures of the S-Trimer subunit vaccine candidate show that it predominately adopts tightly closed pre-fusion state, and resembles that of the native and full-length spike in detergent, confirming its structural integrity. WT S-Trimer is currently being evaluated in global Phase 2/3 clinical trial. Combining with published structures of the S protein, we also propose a model to dissect the conformation change of the spike protein before receptor binding.


Vaccine ◽  
2018 ◽  
Vol 36 (29) ◽  
pp. 4287-4297 ◽  
Author(s):  
Kai Hu ◽  
Ming Fu ◽  
Xinmeng Guan ◽  
Di Zhang ◽  
Xu Deng ◽  
...  

2020 ◽  
Author(s):  
Yangtao Wu ◽  
Xiaofen Huang ◽  
Lunzhi Yuan ◽  
Shaojuan Wang ◽  
Yali Zhang ◽  
...  

AbstractA safe and effective SARS-CoV-2 vaccine is essential to avert the on-going COVID-19 pandemic. Here, we developed a subunit vaccine, which is comprised of CHO-expressed spike ectodomain protein (StriFK) and nitrogen bisphosphonates-modified zinc-aluminum hybrid adjuvant (FH002C). This vaccine candidate rapidly elicited the robust humoral response, Th1/Th2 balanced helper CD4 T cell and CD8 T cell immune response in animal models. In mice, hamsters, and non-human primates, 2-shot and 3-shot immunization of StriFK-FH002C generated 28- to 38-fold and 47- to 269-fold higher neutralizing antibody titers than the human COVID-19 convalescent plasmas, respectively. More importantly, the StriFK-FH002C immunization conferred sterilizing immunity to prevent SARS-CoV-2 infection and transmission, which also protected animals from virus-induced weight loss, COVID-19-like symptoms, and pneumonia in hamsters. Vaccine-induced neutralizing and cell-based receptor-blocking antibody titers correlated well with protective efficacy in hamsters, suggesting vaccine-elicited protection is immune-associated. The StriFK-FH002C provided a promising SARS-CoV-2 vaccine candidate for further clinical evaluation.


2020 ◽  
Author(s):  
Hui Yang ◽  
Haiwen Zhang ◽  
Chenghong Liao ◽  
Jianguo Zhao ◽  
Jinhua Wang ◽  
...  

Abstract such as domestic ducks and geese. Young birds have a high mortality rate after infection. The resistance caused by the abuse of antibiotics is also getting worse. Since there are 25 serotypes of RA, and the cross-immunization between serotypes is weak, it is necessary to find a vaccine that has cross-immunization against multiple serotypes of RA. In this article, the bioinformatics analysis of RA Proin protein was conducted, and it was speculated that it has the potential of a subunit vaccine. The protein was recombinantly expressed and purified, and immunized with Cherry Valley Duck. The results show that the serum antibodies of the Porin protein immunized group were positive at 1:24300 for the porin protein and RA strains CH1. The serum could improve the killing effect of complement and phagocytic cells on RA. After the challenge, the survival rate of Cherry Valley Duck can be increased by 80%.


PLoS ONE ◽  
2012 ◽  
Vol 7 (8) ◽  
pp. e42405 ◽  
Author(s):  
Igor Kolotilin ◽  
Angelo Kaldis ◽  
Bert Devriendt ◽  
Jussi Joensuu ◽  
Eric Cox ◽  
...  

2014 ◽  
Vol 2014 ◽  
pp. 1-10 ◽  
Author(s):  
Katia L. Bacelo ◽  
Daiane D. Hartwig ◽  
Fabiana K. Seixas ◽  
Rodrigo Schuch ◽  
Angelita da S. Moreira ◽  
...  

Leptospiral immunoglobulin-like (Lig) proteins are of great interest due to their ability to act as mediators of pathogenesis, serodiagnostic antigens, and immunogens. Purified recombinant LigA protein is the most promising subunit vaccine candidate against leptospirosis reported to date, however, as purified proteins are weak immunogens the use of a potent adjuvant is essential for the success of LigA as a subunit vaccine. In the present study, we compared xanthan pv. pruni (strain 106), aluminium hydroxide (alhydrogel), and CpG ODN as adjuvants in a LigA subunit vaccine preparation. Xanthan gum is a high molecular weight extracellular polysaccharide produced by fermentation ofXanthomonasspp., a plant-pathogenic bacterium genus. Preparations containing xanthan induced a strong antibody response comparable to that observed when alhydrogel was used. Upon challenge with a virulent strain ofL. interrogansserovar Copenhageni, significant protection (Fisher test,P<0.05) was observed in 100%, 100%, and 67% of hamsters immunized with rLigANI-xanthan, LigA-CpG-xanthan, and rLigANI-alhydrogel, respectively. Furthermore, xanthan did not cause cytotoxicity in Chinese hamster ovary (CHO) cellsin vitro. The use of xanthan as an adjuvant is a novel alternative for enhancing the immunogenicity of vaccines against leptospirosis and possibly against other pathogens.


2014 ◽  
Vol 21 (12) ◽  
pp. 1681-1688 ◽  
Author(s):  
John W. Cherwonogrodzky ◽  
Nicole D. Barabé ◽  
Michelle L. Grigat ◽  
William E. Lee ◽  
Robert T. Poirier ◽  
...  

ABSTRACTA subunit vaccine candidate was produced fromBrucella suis145 (biovar 4; expressing both the A antigen ofBrucella abortusand the M antigen ofBrucella melitensis). The preparation consisted mostly of polysaccharide (PS; >90% [wt/wt]; both cell-associated PS and exo-PS were combined) and a small amount of protein (1 to 3%) with no apparent nucleic acids. Vaccinated mice were protected (these had a statistically significant reduction in bacterial colonization compared to that of unvaccinated controls) when challenged with representative strains of threeBrucellaspecies most pathogenic for humans, i.e.,B. abortus,B. melitensis, andB. suis. As little as 1 ng of the vaccine, without added adjuvant, protected mice againstB. suis145 infection (5 × 105CFU), and a single injection of 1 μg of this subunit vaccine protected mice fromB. suis145 challenge for at least 14 months. A single immunization induced a serum IgG response toBrucellaantigens that remained elevated for up to 9 weeks. The use of heat (i.e., boiling-water bath, autoclaving) in the vaccine preparation showed that it was thermostable. This method also ensured safety and security. The vaccine produced was immunogenic and highly protective against multiple strains ofBrucellaand represents a promising candidate for further evaluation.


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