Functional and structural identification of a new lectin activity of Borrelia recurrentis spirochetes

1. Haemagglutinating activity (HA) was found and characterized in lysate of the spirochete Borrelia recurrentis. 2. The highest HA was observed using native rabbit red blood cells (RBC), especially oxidized rabbit RBC. 3. In a haemagglutination inhibition test the HA showed an affinity with monosaccharides D-glucosamine, D-galactosamine and N-acetyl-D-mannosamine and several glycoproteins and polysaccharides. 4. An inhibitory effect was also achieved by mouse monoclonal antibody H 9724, polyclonal antibodies from B. recurrentis infected mice and with rabbit polyclonal antibodies directed against B. recurrentis HA. 5. B. recurrentis proteins components of 29, 33, 41 and 55 kDa were identified by immunoblotting as structural subunits of complex binding activity of a new agglutinin.