Viridans streptococci have emerged as major opportunistic pathogens. We sug
gest that for these bacteria to proliferate in vivo and cause disease, they
must utilize host tissue components. We have therefore examined he ability
of all recognized species of viridans streptococci to liberate and utilize
the constituent sugars of the glycans of the extensively sialylated human
serum alpha(1)-acid glycoprotein (AGP) as the sole source of carbohydrate t
o support in vitro growth. Analysis of residual glycans following bacterial
growth was performed by high-pH anion exchange chromatography with pulsed
amperometric detection and matrix-assisted laser desorption ionization time
-of-flight mass spectrometry. Only those species which produced sialidase-n
amely, Streptococcus oralis, S. intermedius, and S. defectivus-grew on AGP.
The extent of degradation of glycans was dependent on the particular glyco
sidases produced by the bacteria. S. defectivus produced only a sialidase w
hich released the terminal N-acetylneuraminic acid residues of the glycans,
and the Liberated sugar was utilized. S. intermedius also produced beta-ga
lactosidase and beta-N-acetylglucosaminidase, which removed galactose and N
-acetylglucosamine from desialylated glycans, all of which again were utili
zed by the organism. S, oralis produced beta-galactosidase, beta-N-acetylgl
ucosaminidase, and alpha-fucosidase and novel alpha- and beta-mannosidases
which were apparent only from the analysis of the residual sugars of AGP. S
. oralis cleaved all the sugars from AGP except for 22% of the N-acetylgluc
osamine. The residual N-acetylglucosamine residues remaining were those lin
ked to the asparagine of the peptide backbone. All the monosaccharides rele
ased by S. oralis from AGP, with the exception of fucose, were utilized. Si
alidase production may be a key factor for growth of these species of virid
ans streptococci on glycoproteins in vivo, since they are commonly associat
ed with extra-oral diseases, with S. oralis emerging as an important pathog
en.