ISSN:
1617-4623
Keywords:
Signal sequence
;
Antigenic epitopes
;
Outer membrane protein
;
Immunogenicity
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Summary Fusion proteins comprising the amino-terminal 99 amino acids of the bacteriophage MS2 replicase and various portions of OmpV a major outer membrane protein of Vibrio cholerae were expressed in Escherichia coli K12. These fusions were expressed under the control of the PL promoter of bacteriophage λ, and expression was controlled using a cIts repressor. Fusions occurring within the secretory signal sequence of OmpV gave rise to the production of mature OmpV. The efficiency, however, decreased with progressive deletion of the signal sequence within the fusions. The reactivity of various OmpV fusions with antisera raised against purified OmpV and whole bacteria demonstrated the existence of two antigenic domains: one present in the denatured form and another in the membrane-associated form of OmpV. These domains correspond to markedly hydrophilic regions of the protein as would be predicted for surface-exposed epitopes.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00338089
