Jf. Bohnsack et al., Genetic polymorphisms of group B streptococcus scpB alter functional activity of a cell-associated peptidase that inactivates C5a, INFEC IMMUN, 68(9), 2000, pp. 5018-5025
Many group B Streptococcus agalactiae strains and other pathogenic streptoc
occi express a cell-associated peptidase that inactivates C5a (C5a-ase), th
e major neutrophil chemoattractant produced by activation of the complement
cascade. Type III group B streptococci (GBS) can be classified genotypical
ly into three restriction digest pattern types. Functional C5a-ase activity
of GBS correlates with this genetic typing; therefore, me sought to identi
fy a genetic basis for this phenomenon. Southern hybridization confirms tha
t all type III GBS contain scpB, the gene encoding GBS C5a-ase, GBS strains
with high C5a-ase functional activity and those with no or very low activi
ty both express immunoreactive C5a-ase. The scpB sequence of strain 130, wh
ich has high C5a-ase activity, is 98.2% homologous to the previously report
ed serotype II GBS scpB sequence. The scpB sequences of strains I25 and GW,
which have low or no C5a-ase activity, are identical. The predicted I25 an
d GW C5a-ase proteins share a four-amino-acid deletion affecting the protea
se histidine active-site consensus motif. Recombinant I30 C5a-ase has good
functional activity, whereas recombinant I25 C5a-ase has low activity. Thes
e data demonstrate that functional C5a-ase differences between type III GBS
strains are attributable to a genetic polymorphism of scpB. The ubiquitous
expression of C5a-ase, irrespective of functional activity, suggests that
C5a-ase may have a second, as yet unidentified, function.