The importance of pathogenic fungi in the context of human health has increased dramatically over the last few decades. This is primarily due to a rise in the number of people suffering from conditions that affect immune competence. Very few options for treatment exist, and the mortality from systemic fungal disease remains very high (commonly more than 50%). The close evolutionary relationship between fungi and humans, which scientists have exploited extensively by using model systems such as Saccharomyces cerevisiae and Schizosaccharomyces pombe to understand eukaryotic biology, is prohibitive for designing safe therapies. Most of the current antifungal drugs exploit differences in fungal and animal membranes, and the absence of the cell wall on host cells. Mitochondrial function has been implicated in antifungal drug susceptibility and virulence of human fungal pathogens. It is interesting that there are several fungal mitochondrial proteins that do not have close homologs in animals. However, despite being a potential source of pathogen-specific targets for future antifungal therapies, the function of mitochondria in fungal pathogens is largely understudied. We are studying the mitochondrial ERMES (Endoplasmic Reticulum Mitochondria Encounter Structure) complex in the major human pathogen Candida albicans. This complex is widely conserved in fungi, but not present in animals. In S. cerevisiae, ERMES has been shown to consists of five subunits (Mmm1, Mdm10, Mdm12, Mdm34 and Gem1), which act to tether the endoplasmic reticulum and mitochondrial membrane systems presumably to enable exchange between the two organelles. We show that in C. albicans the ERMES complex is critical for fitness and the growth defect is more pronounced at host body temperature of 37°C. These phenotypes are encouraging for considering this complex for future drug design. Consistent with the S. cerevisiae studies, the C. albicans ERMES mutants display mitochondrial DNA loss and mitochondrial morphology defects. Current studies involve the biochemical characterisation of the complex and its relationship to other protein machines in the mitochondrial outer membrane, as well as deciphering the role of ERMES in lipid homeostasis in C. albicans and understanding the basis for its essential cellular function.