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Expression of an inaccessible P1.7 subtype epitope on meningococcal class 1 proteins

E. Wedege, R. Dalseg, D. A. Caugant, J. T. Poolman^* and L. O. Frholm

National Institute of Public Health, Geitmyrsveien 75, 0462 Oslo 4, Norway

^*National Institute of Public Health and Environmental Protection, Antonie van Leeuwenhoeklaan 9, PO Box 1, 3720 BA Bilthoven, The Netherlands

Received December 9, 1991 Revision received April 30, 1992.
Accepted April 30, 1992

Dot-blot analysis of whole-cell suspensions of meningococci showed that 81% of B:15:P1.16 strains from patients reacted with a monoclonal antibody (MAb) against subtype P1.7. The remaining strains, which did not react on dot-blots or in ELISA, demonstrated the P1.7 subtype epitope on immunoblots after denaturation of the cells with sodium dodecyl sulphate. The monomeric class 1 proteins of the two P1.16 subtype variants had slightly different mol. wts, but bound the P1.7 antibody equally well. These results were explained by a deletion of three codons in the gene encoding the first variable region of the P1.16 class 1 protein. The deletion accounted for the non-exposure of the P1.7 epitope on native cells. Other patient strains, with subtypes P1.3, P1.9 or without any known subtype, also showed a binding site for the P1.7 MAb, which became available only after denaturation. Demonstration of inaccessible epitopes may have consequences for subtype designations and vaccine development.

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