PhoE protein as a carrier for foreign epitopes.
Outer membrane protein PhoE of E. coli appears to be a suitable carrier for the expression of foreign antigenic determinants at the bacterial cell-surface. Insertion of stretches of amino acids in the cell-surface exposed regions of PhoE does not interfere with the biogenesis of the protein. Dependent on the cell-surface exposed loop used for insertion and the character of the inserted amino acids up to 50 amino acids could be inserted. Both B-cell epitopes and T-cell epitopes remain antigenic and immunogenic in the PhoE-associated conformation. However, flanking amino acids can interfere with the antigenicity and immunogenicity of T-cell epitopes inserted in PhoE. Because E. coli PhoE can be expressed in attenuated Salmonella and Shigella strains, it seems to be a suitable vaccine carrier candidate.
Janssen
R
R
Department of Molecular Cell Biology, Utrecht University, The Netherlands.
Tommassen
J
J
D000595:Amino Acid Sequence; D000818:Animals; D001402:B-Lymphocytes / Q000276:immunology; D001428:Bacterial Vaccines / Q000276:immunology; D000939:Epitopes / Q000096:biosynthesis / Q000276:immunology*; D029968:Escherichia coli Proteins; D008969:Molecular Sequence Data; D018272:Porins / Q000276:immunology*; D011487:Protein Conformation; D011993:Recombinant Fusion Proteins; D013601:T-Lymphocytes / Q000276:immunology*
D001428:Bacterial Vaccines; D000939:Epitopes; D029968:Escherichia coli Proteins; D018272:Porins; D011993:Recombinant Fusion Proteins; C082922:PhoE protein, E coli