The N-acetylglucosaminidase of Candida albicans is a secreted hydrolyt
ic enzyme that contributes to the yeast's virulence. There was a signi
ficant increase in the N-acetylglucosaminidase activity of C. albicans
cells released from carbon starvation in medium containing N-acetylgl
ucosamine. The increased enzyme activity in N-acetylglucosamine-grown
cells correlated with increased transcription of the HEX1 gene, which
encodes C. albicans N-acetylglucosaminidase. In contrast, glucose repr
essed HEX1 transcription, and glucose-grown cells had on average 94-fo
ld lower N-acetylglucosaminidase activities than did N-acetylglucosami
ne-grown cells. N-acetylglucosaminidase induction in cells grown on N-
acetylglucosamine was also repressed by fructose, mannose or galactose
, although to a lesser extent than by glucose, and sucrose repressed e
nzyme production by only 10%. Eighty-eight percent of the enzyme in N-
acetylglucosamine-grown cells was localised in the periplasm, and afte
r incubation for 5 h, 30 or 70% of the total enzyme activity was secre
ted into the medium by yeast or mycelial cells, respectively. The cell
ular location of the enzyme and the regulation of production by the ca
rbon source indicate a scavenging role for C. albicans N-acetylglucosa
minidase.