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Published on: July 25, 2022
Immunogenicity of recombinant class 1 protein from Neisseria meningitidis refolded into phospholipid vesicles and
O Niebla1, A Alvarez, A Martín
1Division of Vaccines, Centre for Genetic Engineering and Biotechnology, PO Box 6162, Ave 31, Apartado 6162, 10600, La Havana, Cuba.
Abstract:
The possibility of eliciting bactericidal antibodies against a recombinant class 1 protein (P1) from Neisseria meningitidis, joined to the first 45 amino acids of the neisserial LpdA protein (PM82), was examined. P1 was produced in Escherichia coli as intracellular inclusion bodies, from which it was purified and reconstituted by (a) inclusion into phospholipid vesicles and detergent and (b) refolding in 0.1% SDS. When Balb/c mice were immunised, high titres of subtype-specific bactericidal antibodies against P1 were obtained in both cases. These results suggest that in spite of being a denaturing agent, it is possible to use SDS to reconstitute the P1 protein in a conformation that exposes the immunodominat regions.
