Characterization of Candida parapsilosis infection of an in vitro reconstituted human oral epithelium.
Oral candidosis is a common problem in immunocompromised patients, and whilst Candida albicans is regarded as the principal cause of infection, other non-Candida albicans Candida (NCAC) species are increasingly being recognized as human pathogens. Relatively little is known about the virulence factors associated with NCAC species, and the aim of this study was to use a reconstituted human oral epithelium (RHOE) to examine epithelial infection withCandida parapsilosis. Strains originating from the oral and vaginal mucosa and from the urinary tract were all shown to colonize RHOE in a strain-dependent manner. Strain differences were found in the colonizing morphology and in the extent of invasion of the RHOE. Low invasion of RHOE was detected for strains after 12 h, whereas extensive tissue damage was evident after 24 h when assessed using histological examination and lactate dehydrogenase activity determination. Tissue damage was reduced in the presence of pepstatin A, although C. parapsilosis invasion of the tissue was not inhibited. Real-time polymerase chain reaction of secreted aspartyl proteinase (SAP) genes (SAPP1-3) showed that expression was strain dependent, with an increased expression generally occurring for Candida infecting RHOE compared with planktonic equivalents. In summary, C. parapsilosis was not highly invasive of RHOE but did induce significant tissue damage, which could relate to specific SAPgene expression.
Silva
Sónia
S
Institute for Biotechnology and Bioengineering, Universidade do Minho, Braga, Portugal.
Henriques
Mariana
M
Oliveira
Rosário
R
Azeredo
Joana
J
Malic
Sladjana
S
Hooper
Samuel J
SJ
Williams
David W
DW
D016282:Aspartic Acid Endopeptidases / Q000032:analysis; D002175:Candida / Q000145:classification / Q000201:enzymology / Q000472:pathogenicity*; D002177:Candidiasis / Q000382:microbiology; D002180:Candidiasis, Oral / Q000201:enzymology / Q000382:microbiology*; D002181:Candidiasis, Vulvovaginal / Q000382:microbiology; D004848:Epithelium / Q000201:enzymology / Q000382:microbiology; D005260:Female; D005656:Fungal Proteins / Q000032:analysis; D006801:Humans; D007770:L-Lactate Dehydrogenase / Q000032:analysis; D018613:Microscopy, Confocal; D008855:Microscopy, Electron, Scanning; D009061:Mouth Mucosa / Q000201:enzymology / Q000382:microbiology*; D010436:Pepstatins / Q000494:pharmacology; D016133:Polymerase Chain Reaction; D011480:Protease Inhibitors / Q000494:pharmacology; D013997:Time Factors; D014552:Urinary Tract Infections / Q000382:microbiology; D014774:Virulence
D005656:Fungal Proteins; D010436:Pepstatins; D011480:Protease Inhibitors; D007770:L-Lactate Dehydrogenase; D016282:Aspartic Acid Endopeptidases; C086390:SAP1 protein, Candida albicans; C090753:SAP2 protein, Candida; C090754:SAP3 protein, Candida albicans; C031375:pepstatin