A novel recombinant bivalent outer membrane protein of Vibrio vulnificus and Aeromonas hydrophila as a vaccine antigen of American eel (Anguilla rostrata)

2015 ◽  
Vol 43 (2) ◽  
pp. 477-484 ◽  
Author(s):  
Guo SongLin ◽  
Lu PanPan ◽  
Feng JianJun ◽  
Zhao JinPing ◽  
Lin Peng ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Aeromonas Hydrophila ◽  
Vibrio Vulnificus ◽  
Vaccine Antigen ◽  
Anguilla Rostrata ◽  
American Eel

scholarly journals Antigenic Structure of Outer Membrane Protein E ofMoraxella catarrhalis and Construction and Characterization of Mutants

2000 ◽  
Vol 68 (11) ◽  
pp. 6250-6256 ◽  
Author(s):  
Timothy F. Murphy ◽  
Aimee L. Brauer ◽  
Norine Yuskiw ◽  
Thomas J. Hiltke
Keyword(s):  
Monoclonal Antibodies ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Vaccine Antigen ◽  
Antigenic Structure ◽  
Effective Vaccine ◽  
Fusion Peptides ◽  
Bacterial Surface ◽  
Normal Human

ABSTRACT Outer membrane protein E (OMP E) is a 50-kDa protein ofMoraxella catarrhalis which possesses several characteristics indicating that the protein will be an effective vaccine antigen. To study the antigenic structure of OMP E, eight monoclonal antibodies were developed and characterized. Three of the antibodies recognized epitopes which are present on the bacterial surface. Fusion peptides corresponding to overlapping regions of OMP E were constructed, and immunoblot assays were performed to localize the areas of the molecule bound by the monoclonal antibodies. These studies identified a surface-exposed epitope in the region of amino acids 80 through 180. To further study the protein, two mutants which lack OMP E were constructed. In bactericidal assays, the mutants were more readily killed by normal human serum compared to the isogenic parent strains. These results indicate that OMP E is involved in the expression of serum resistance of M. catarrhalis.

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