Molecular identification and antigenic characterization of Babesia divergens Erythrocyte Binding Protein (BdEBP) as a potential vaccine candidate

2017 ◽  
Vol 66 (6) ◽  
pp. 721-726 ◽  
Author(s):  
Shimaa Abd El-Salam El-Sayed ◽  
Mohamed Abdo Rizk ◽  
Mohamad Alaa Terkawi ◽  
Naoaki Yokoyama ◽  
Ikuo Igarashi
2022 ◽  
Vol 8 ◽  
Author(s):  
Shimaa Abd El-Salam El-Sayed ◽  
Mohamed Abdo Rizk ◽  
Haitham Eldoumani ◽  
Shimaa Sobhy Sorour ◽  
Mohamad Alaa Terkawi ◽  
...  

The molecular identification and antigenic characterization of P0 protein in Babesia divergens, a blood parasite of veterinary and zoonotic importance, were carried out in this study for use in developing subunit vaccines against B. divergens infection. Recombinant protein encoding P0 (BdP0) was developed in Escherichia coli, and its antiserum was generated in mice for further molecular characterization. Anti-rBdP0 serum had a specific interaction with the corresponding legitimate B. divergens protein, as confirmed by Western blotting and indirect fluorescent antibody tests. ELISA was used to assess the immunogenicity of BdP0 in a group of 68 bovine field samples, and significant immunological reactivity was found in 19 and 20 positive samples of rBdp0 and B. divergens lysate, respectively. The in vitro growth of B. divergens cultures treated with anti-rBdP0 serum was significantly inhibited (p < 0.05). Furthermore, after 6 h of incubation with 2 mg/ml anti-rBdP0 serum, the ability of pre-incubated free merozoites to invade bovine erythrocytes was reduced by 59.88%. The obtained data suggest the possible use of rBdP0 as diagnostic antigen and may serve as a vaccine candidate against babesiosis caused by B. divergens either in animal or human.


2017 ◽  
Vol 48 (1) ◽  
Author(s):  
Yanqing Bao ◽  
Mingxing Tian ◽  
Peng Li ◽  
Jiameng Liu ◽  
Chan Ding ◽  
...  

Author(s):  
Pothiaraj Govindan ◽  
Packiyadass Manjusha ◽  
Konda Mani Saravanan ◽  
Vijayakumar Natesan ◽  
Saleh H. Salmen ◽  
...  

Biologia ◽  
2021 ◽  
Author(s):  
Elham Mehdizadeh Marzenaki ◽  
Ali Reza Saeedinia ◽  
Mehdi Zeinoddini ◽  
Ali Asghar Deldar

2005 ◽  
Vol 73 (11) ◽  
pp. 7569-7577 ◽  
Author(s):  
Daxin Peng ◽  
Wenzhou Hong ◽  
Biswa P. Choudhury ◽  
Russell W. Carlson ◽  
Xin-Xing Gu

ABSTRACT Lipooligosaccharide (LOS) is a major surface component of Moraxella catarrhalis and a possible virulence factor in the pathogenesis of human infections caused by this organism. The presence of LOS on the bacterium is an obstacle to the development of vaccines derived from whole cells or outer membrane components of the bacterium. An lpxA gene encoding UDP-N-acetylglucosamine acyltransferase responsible for the first step of lipid A biosynthesis was identified by the construction and characterization of an isogenic M. catarrhalis lpxA mutant in strain O35E. The resulting mutant was viable despite the complete loss of LOS. The mutant strain showed significantly decreased toxicity by the Limulus amebocyte lysate assay, reduced resistance to normal human serum, reduced adherence to human epithelial cells, and enhanced clearance in lungs and nasopharynx in a mouse aerosol challenge model. Importantly, the mutant elicited high levels of antibodies with bactericidal activity and provided protection against a challenge with the wild-type strain. These data suggest that the null LOS mutant is attenuated and may be a potential vaccine candidate against M. catarrhalis.


PLoS ONE ◽  
2013 ◽  
Vol 8 (10) ◽  
pp. e77394 ◽  
Author(s):  
Gajalakshmi Dakshinamoorthy ◽  
Gnanasekar Munirathinam ◽  
Kristen Stoicescu ◽  
Maryada Venkatarami Reddy ◽  
Ramaswamy Kalyanasundaram

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