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Antibodies raised in animals against the Streptococcus agalactiae proteins c and R4 and normal human serum antibodies target distinct epitopes

¹Department of Medical Microbiology, Faculty of Medicine, University of Zimbabwe Medical School, PO Box A178, Avondale, Harare, Zimbabwe ²Department of Laboratory Medicine, Children's and Women's Health, Norwegian University of Science and Technology, N-7006 Trondheim, Norway

Correspondence Johan A. Maeland Johan.Meland{at}medisin.ntnu.no

Received October 3, 2002
Accepted January 29, 2003

The targets for normal human serum antibodies that react with proteins c and R4 isolated from group B streptococci (GBS; Streptococcus agalactiae) have been studied and compared with the targets for murine monoclonal and rabbit polyclonal antibodies raised against these proteins. The proteins were extracted by trypsin digestion and purified by precipitations and gel filtration and testing was based on enzyme immunoassays. The immune antibodies showed specificity for the corresponding protein, targeted that protein in Western blotting and recognized their targets after heat treatment (100 °C) of the proteins. Human antibodies in a commercial gammaglobulin preparation targeted a site(s) common to c and R4. This target failed to bind the antibodies in Western blotting and was destroyed by heating. c- and R4-reactive antibodies in sera from healthy pregnant women recognized the common, heat-labile determinant(s), but contained little or no antibodies against the heat-stable c- or R4-specific determinants. These results are consistent with the notions that (i) the normal human antibodies and the immunization-induced animal antibodies targeted different sites on the c and R4 proteins and that (ii) the natural human antibodies targeted conformational epitopes and the immune antibodies targeted linear epitopes. These findings are important for further clarification of GBS immunology and immunoprotection in humans.

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