Calcium-dependent ESCRT recruitment and lysosome exocytosis maintain epithelial integrity during Candida albicans invasion.

Candida albicans is both a commensal and an opportunistic fungal pathogen. Invading hyphae of C. albicans secrete candidalysin, a pore-forming peptide toxin.

Maintaining phagosome integrity during fungal infection: do or die?

Professional phagocytes represent a critical node in innate immunity and tissue homeostasis through their specialized ability to eat, drink, and digest material from the extracellular milieu. The degradative and microbicidal functions of phagocytes rely on the fusion of lysosomes with endosomal compartments such as phagosomes, resulting in the digestion and recycling of internalized prey and debris. Despite these efforts, several particularly dangerous infections result from a class of tenacious pathogens that resist digestion, often surviving and even proliferating within the confines of the phagosomal membrane.

Genes encoding a striatin-like protein (ham-3) and a forkhead associated protein (ham-4) are required for hyphal fusion in Neurospora crassa.

Cell-cell fusion during fertilization and between somatic cells is an integral process in eukaryotic development. In Neurospora crassa, the hyphal anastomosis mutant, ham-2, fails to undergo somatic fusion. In both humans and Saccharomyces cerevisiae, homologs of ham-2 are found in protein complexes that include homologs to a striatin-like protein and a forkhead-associated (FHA) protein.