Streptococcus agalactiae
(Group B streptococcus, GBS) is a leading cause of infections in neonates and an emerging pathogen in adults. The Lancefield Group B carbohydrate (GBC) is a peptidoglycan-anchored antigen that defines this species as a Group B Streptococcus. Despite earlier immunological and biochemical characterizations, the function of this abundant glycopolymer has never been addressed experimentally. Here, we inactivated the gene
gbcO
encoding a putative UDP-N-acetylglucosamine-1-phosphate:lipid phosphate transferase thought to catalyze the first step of GBC synthesis. Indeed, the
gbcO
mutant was unable to synthesize the GBC polymer, and displayed an important growth defect
in vitro
. Electron microscopy study of the GBC-depleted strain of
S. agalactiae
revealed a series of growth-related abnormalities: random placement of septa, defective cell division and separation processes, and aberrant cell morphology. Furthermore, vancomycin labeling and peptidoglycan structure analysis demonstrated that, in the absence of GBC, cells failed to initiate normal PG synthesis and cannot complete polymerization of the murein sacculus. Finally, the subcellular localization of the PG hydrolase PcsB, which has a critical role in cell division of streptococci, was altered in the
gbcO
mutant. Collectively, these findings show that GBC is an essential component of the cell wall of
S. agalactiae
whose function is reminiscent of that of conventional wall teichoic acids found in
Staphylococcus aureus
or
Bacillus subtilis
. Furthermore, our findings raise the possibility that GBC-like molecules play a major role in the growth of most if not all beta –hemolytic streptococci.