Disease relevance of VMA7

• A recombinant form of Vma7p was expressed in Escherichia coli and purified to homogeneity [1].
• The vma7 null mutant strains were avirulent in a mouse model of systemic candidiasis [2].

High impact information on VMA7

• Although Vma7p and Vma10p have been observed to interact with the V0 sector, our results indicate that these subunits behave primarily as canonical V1 sector subunits [3].
• Epitope-tagged Vma7p was constructed and the proton uptake activity of isolated vacuoles from this yeast strain was markedly inhibited by a monoclonal antibody against the epitope-tag [4].
• Vacuolar membranes isolated from a vma7 delta null mutant contained no V-ATPase activity [5].
• Western analysis of vma7 delta cells revealed greatly reduced levels of the remaining V0 complex V-ATPase subunits, but normal levels of the V1 subunits [5].
• The putative vacuolar ATPase subunit Vma7p of Candida albicans is involved in vacuole acidification, hyphal development and virulence [2].

Biological context of VMA7

• In summary, the V-ATPase subunit Vma7p is involved in vacuolar ion transport and this transport is required for hyphal growth and virulence of C. albicans [2].
• In addition, C. albicans vma7 null mutants and the null mutant strain of the Vma7p-interacting phosphatidylinositol 3-kinase Vps34p showed similar phenotypes [2].

Physical interactions of VMA7

• The phosphatidylinositol 3-kinase Vps34p of the human pathogenic yeast Candida albicans is a multifunctional protein that interacts with the putative vacuolar H+ -ATPase subunit Vma7p [6].

Other interactions of VMA7

• The anti-HA epitope antibody inhibited both the ATP-dependent proton uptake and the ATPase activities of the Vma16p-HA and Vma7p-HA containing complexes, in intact vacuoles and in the detergent-solubilized enzyme [7].
• In order to characterize the functional link between these two activities we searched for proteins interacting with C. albicans Vps34p and demonstrate physical interaction of Vps34p with the subunit of the vacuolar H+ -ATPase Vma7p [6].

Analytical, diagnostic and therapeutic context of VMA7

• Analysis of secondary structure by circular dichroism and FTIR showed that Vma7p comprises 30% alpha-helix and 32-42% beta-sheet [1].

References