MycoBiomDB – Record Details (MyCo_5663)

Biomarker Record Details

Database ID: MyCo_5663
DB IDMyCo_5663
TitleHyphal Als proteins act as CR3 ligands to promote immune responses against Candida albicans
Year2024
PMID38724513
Fungal Diseases involvedInvasive candidiasis
Associated Medical ConditionNone
GenusCandida
Speciesalbicans
OrganismCandida albicans
Ethical StatementAll studies described have been approved by UC Irvine oversight committees, including the use of mice as a source of macrophages and dendritic cells by the UC Irvine IACUC. The mouse systemic infection studies were approved by the Institutional Animal Care and Use Committee at the Lundquist Institute for Biomedical Innovation at Harbor-UCLA Medical Center.
Site of InfectionNone
Opportunistic invasiveInvasive
Sample typeBiopsy
Sample sourceExtracted tissue
Host GroupAnimal
Host Common nameMice
Host Scientific nameMus musculus
Biomarker NameAls3
Biomarker Full NameAls3
Biomarker TypeDiagnostic
BiomoleculeProtein
Geographical LocationUSA
CohortCD18−/− mice were originally provided by Claire Doerschuk (University of North Carolina, Chapel Hill, NC, USA). Dectin-2-de cient mice were a kind gift from Yoichiro Iwakura (University of Tokyo, Tokyo, Japan). Age- and sex-matched C57BL/6 J mice were purchased from Jackson Laboratories (Bar Harbor, ME, USA). 6-week-old male and female C57BL/6 J mice were purchased for in vivo experiments.
Cohort No.None
Age GroupNone
P ValueNone
SensitivityNone
SpecificityNone
Positive Predictive ValueNone
MICNone
Fold ChangeNone
PathwayNone
Disease Introduction MechanismInvasive candidiasis, caused mainly by the opportunistic fungus Candida albicans, is a leading cause of nosocomial bloodstream infection in developed countries, with a mortality that can exceed 40% despite antifungal treatment1. The limited ef cacy of antifungal drugs and the rising incidence of antifungal resistance indicate a need to develop new therapies for invasive candidiasis1. Opportunistic“high-damaging” C. albicans strains produce toxic factors, such as pore-forming candidalysin, aspartyl proteases (Saps), and the agglutinin-like sequence (Als) proteins, during the transition from benign commensal yeasts to pathogenic hyphae, exacerbating in ammation2–5. Compared to yeasts, hyphae cause more tissue damage, both directly via candida-lysin and Saps and indirectly by exacerbating the in amatory responses. However, the interactions between hyphae and myeloid cells that drive antifungal immunity remain poorly understood.
TechniquePCR
Analysis MethodqRT-PCR
ELISA kitsNone
Assay DataNone
Validation Techniques usedqRT-PCR
Up Regulation Down RegulationPositive
Sequence DataNone
External LinkNone