Candida albicans Pathogenicity and Epithelial Immunity

Naglik, Julian R.; Richardson, Jonathan P.; Moyes, David L.

doi:10.1371/journal.ppat.1004257

Cited by 89 publications

(63 citation statements)

References 17 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Therefore, these signalling pathways may enable different mucosal tissues to detect fungal hyphae, thereby potentially identifying when certain Candida species have become pathogenic. Notably, epithelial activation by Candidalysin is not mediated via C-type lectin receptors (CLRs) or Toll-like receptors (TLRs) [2], suggesting that epithelial cells utilise different sensing mechanisms than myeloid cells; whereby myeloid cells respond to C. albicans cell wall moieties (β-glucan and mannans) (see below) and epithelial cells respond to damage-inducing C. albicans through p38/c-Fos/MKP1 by detecting Candidalysin activity [25–27]. Similar p38 activation has been observed in murine intestinal epithelial cells with bacterial pathogens ( Citrobacter rodentium ) [28] and in C. elegans (nematode worm) with C. albicans [29], indicating that p38 signalling may be a common epithelial mechanism for the detection of pathogenic microbes.…”

Section: Epithelial Damage and Immune Activation By Candidalysinmentioning

confidence: 99%

Candida albicans–epithelial interactions and induction of mucosal innate immunity

Naglik

König

Hube

et al. 2017

Current Opinion in Microbiology

113

112

View full text Add to dashboard Cite

Candida albicans is a human fungal pathogen that causes millions of mucosal and life-threatening infections annually. C. albicans initially interacts with epithelial cells, resulting in fungal recognition and the formation of hyphae. Hypha formation is critical for host cell damage and immune activation, which are both driven by the secretion of Candidalysin, a recently discovered peptide toxin. Epithelial activation leads to the production of inflammatory mediators that recruit innate immune cells including neutrophils, macrophages and innate Type 17 cells, which together work with epithelial cells to clear the fungal infection. This review will focus on the recent discoveries that have advanced our understanding of C. albicans-epithelial interactions and the induction of mucosal innate immunity.

show abstract

Section: Epithelial Damage and Immune Activation By Candidalysinmentioning

confidence: 99%

Candida albicans–epithelial interactions and induction of mucosal innate immunity

Naglik

König

Hube

et al. 2017

Current Opinion in Microbiology

113

112

View full text Add to dashboard Cite

show abstract

“…In the context of the host, C. albicans is exposed to numerous physical and chemical signals that can trigger a variety of responses, including morphological transitions between yeast and filamentous forms, switching between different cell types, the formation of multicellular structures, including biofilms, and altered cell wall states (6)(7)(8)(9). The ability of C. albicans to respond to different stimuli contributes to its virulence (3).…”

mentioning

confidence: 99%

Analysis of the Candida albicans Phosphoproteome

et al. 2015

View full text Add to dashboard Cite

dCandida albicans is an important human fungal pathogen in both immunocompetent and immunocompromised individuals. C. albicans regulation has been studied in many contexts, including morphological transitions, mating competence, biofilm formation, stress resistance, and cell wall synthesis. Analysis of kinase-and phosphatase-deficient mutants has made it clear that protein phosphorylation plays an important role in the regulation of these pathways. In this study, to further our understanding of phosphorylation in C. albicans regulation, we performed a deep analysis of the phosphoproteome in C. albicans. We identified 19,590 unique peptides that corresponded to 15,906 unique phosphosites on 2,896 proteins. The ratios of serine, threonine, and tyrosine phosphosites were 80.01%, 18.11%, and 1.81%, respectively. The majority of proteins (2,111) contained at least two detected phosphorylation sites. Consistent with findings in other fungi, cytoskeletal proteins were among the most highly phosphorylated proteins, and there were differences in Gene Ontology (GO) terms for proteins with serine and threonine versus tyrosine phosphorylation sites. This large-scale analysis identified phosphosites in protein components of Mediator, an important transcriptional coregulatory protein complex. A targeted analysis of the phosphosites in Mediator complex proteins confirmed the large-scale studies, and further in vitro assays identified a subset of these phosphorylations that were catalyzed by Cdk8 (Ssn3), a kinase within the Mediator complex. These data represent the deepest single analysis of a fungal phosphoproteome and lay the groundwork for future analyses of the C. albicans phosphoproteome and specific phosphoproteins.

show abstract

“…High rate of Candida proliferation is also associated with some gut diseases containing Crohn's disease and ulcerative colitis, which can decrease fungal burdens and alleviate disease intensity [13].…”

Section: Objectivementioning

confidence: 99%