Properties and distribution of the putative R3 protein of <i>Streptococcus agalactiae</i>

Abstract

Strain-variable Streptococcus agalactiae (group B streptococci; GBS) proteins exposed at the bacterial cell surface are important markers in GBS serotyping. These proteins include the c proteins c(alpha) and c(beta) and the R proteins R1 through R4, of which R1 and R4 have been studied most extensively. This study presents the characteristics of a protein which was expressed by a capsular antigen type V GBS strain shown by means of polyclonal and monoclonal antibody testing. Examination of a number of reference and prototype strains by fluorescent antibody testing and Western blotting provided evidence that the serotype V-derived protein was the R3 protein of GBS, previously defined on the basis of immunoprecipitation assays. The putative R3 protein formed ladder-like banding patterns on Western blotting with polypeptides in the 30 kDa to > or = 140 kDa range, was destroyed by pepsin digestion, and partially degraded by trypsin digestion. The protein was expressed by 10 (6.5%) of 153 clinical GBS strains tested, the expression being restricted to isolates of the capsular antigen types II, III, and V. Some isolates expressed both the c(beta) and the R3 protein. Expression in combination with c(alpha) or R4 protein synthesis was not detected. Inclusion of the anti-R3 monoclonal antibody among antibody reagents for GBS serotyping will enhance the discriminatory power of this typing method.