Bevanger, L., Kvam. A. I. & Mdand, J. A. A Streptococcus agulactiue R protein analysed by polyclonal and monoclonal antibodies. APMIS 103: 731-736, 1995. Unexpected cross-reactivity between two Streptococcus uguluctiue (GBS) isolates formed the basis for purification of a GBS protein called the Ra antigen, and raising of murine monoclonal antibody (MAb) against Ra. The Ra protein was resistant to trypsin digestion, susceptible to pepsin digestion, formed a ladder-like pattern of lines with a periodicity of -8 kD on immunoblotting, was surfacelocalized in GBS strains, and was variably expressed by GBS. These characteristics provided evidence that the Ra antigen belonged to the R proteins of GBS. By testing of reference GBS isolates and antiserum, including an anti-R4 protein serum, cross-reactivity was recorded consistent with the assumption that Ra is a R4 protein. The Ra/R4 protein also showed cross-reactivity with a previously described GBS protein called protein Rib (J. Exp. Med. 177: 1593-1603, 1993. Several characteristics of the RdR4 protein were similar to those of the GBS protein ca, but the two proteins showed no cross-reactivity. The anti-RdR4 MAb has proved useful in serosubtype determination of GBS of known serotype and should be a valuable tool for studying the immunobiological function of antibodies targetting the surface-localized Ra/R4 protein.Streptococcus agalactiae (group B streptococci; GBS) are important pathogens in humans, particularly in neonatal infections. The bacteria harbour capsular carbohydrate antigens which for decades have formed the basis for serotype determination, and have also been considered important virulence factors of GBS and targets for protective antibodies (1, 2). In addition to the serotype antigen, the majority of GBS isolates harbour surface-localized protein antigens which show strain variability. Of these, the ca and cp antigens of the c proteins and the R protein antigens have attracted considerable interest (7, 11, 12). These proteins provide the basis
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