The role of secreted aspartyl proteinases in Candida tropicalis invasion and damage of oral mucosa.
Candida virulence attributes include the ability to colonize and invade host tissues, and the secretion of hydrolytic enzymes. Although Candida albicans is regarded as the principal fungi causing infections in humans, other species, particularly Candida tropicalis, are increasingly being recognized as human pathogens. Relatively little is known, however, about the virulence attributes associated with C. tropicalis. The present study aimed to investigate epithelial infection by C. tropicalis using a reconstituted human oral epithelium (RHOE) together with confocal laser scanning microscopy and real-time PCR. A comparison of clinical strains was made in terms of tissue colonization, invasion and C. tropicalis secreted aspartyl proteinase (SAPT) gene expression. All C. tropicalis strains were able to colonize RHOE in a strain-dependent manner. After 12 h of infection, C. tropicalis was found to be highly invasive, with extensive tissue damage occurring after 24 h. Real-time PCR of C. tropicalis SAPT1-4 genes showed that expression was strain-dependent, with SAPT2-4 transcripts being frequently detected and SAPT1 rarely detected. Tissue invasion and damage was not inhibited by the presence of pepstatin A. Accordingly, and given that an increase in infection time was not accompanied with an increase in SAPT gene expression, it can be suggested that the proteinases are not involved in invasion and damage of RHOE by C. tropicalis. In summary, C. tropicalis can be considered as highly invasive with the ability to induce significant tissue damage. These features, however, do not appear to be related to specific SAPT gene expression.
Silva
S
S
Institute for Biotechnology and Bioengineering, Universidade do Minho, Campus de Gualtar, Braga, Portugal.
Hooper
S J
SJ
Henriques
M
M
Oliveira
R
R
Azeredo
J
J
Williams
D W
DW
D057055:Aspartic Acid Proteases / Q000378:metabolism*; D041022:Candida tropicalis / Q000201:enzymology* / Q000472:pathogenicity*; D006801:Humans; D018613:Microscopy, Confocal; D009061:Mouth Mucosa / Q000382:microbiology* / Q000473:pathology*; D016133:Polymerase Chain Reaction; D037521:Virulence Factors / Q000378:metabolism*
D037521:Virulence Factors; D057055:Aspartic Acid Proteases