An immunogenic loop within the diphtheria toxin has been deleted from
the B-subunit by a modification of the inverse polymerase chain reacti
on (IPCR) and replaced by a unique restriction endonuclease site. An o
ligonucleotide encoding an identified epitope sequence from the major
outer membrane protein of Neisseria meningitidis of similar size and s
tructure to that deleted has been introduced into the restriction site
. Expression of the resulting chimeric B-subunit from Escherichia coil
yielded a protein that was recognised by a panel of antibodies specif
ic for the meningococcal epitope. Initial immunisation data suggest th
at this protein could elicit an antibody response against both diphthe
ria toxin and meningococcal proteins.