Immunogenicity of recombinant class 1 protein from Neisseria meningitidis refolded into phospholipid vesicles and detergent

The possibility of eliciting bactericidal antibodies against a recombinant class 1 protein (P1) from Neisseria meningitidis, joined to the first 45 am ino acids of the neisserial LpdA protein (PM82), was examined. P1 was produ ced in Escherichia coli as intracellular inclusion bodies, from which it wa s purified and reconstituted by (a) inclusion into phospholipid vesicles an d detergent and (b) refolding in 0.1% SDS. When Balb/c mice were immunised, high titres of subtype-specific bactericidal antibodies against P1 were ob tained in both cases. These results suggest that in spite of being a denatu ring agent, it is possible to use SDS to reconstitute the P1 protein in a c onformation that exposes the immunodominat regions. (C) 2001 Elsevier Scien ce Ltd. All rights reserved.