Functional and Structural Diversity in the Als Protein Family ofCandida albicans

摘要: The human fungal pathogen Candida albicans colonizes and invades a wide range of host tissues. Adherence to constituents plays an important role in this process. Two members the C. Als protein family (Als1p Als5p) have been found mediate adherence; however, functions other are unknown. In study, ALS gene were cloned expressed Saccharomyces cerevisiae characterize their individual functions. Distinct proteins conferred distinct adherence profiles diverse substrates. Using chimeric Als5p-Als6p constructs, regions mediating substrate-specific localized N-terminal domains proteins. Interestingly, subset also mediated endothelial cell invasion, previously unknown function family. Consistent with these results, homology modeling revealed that contain anti-parallel β-sheet motifs interposed by extended regions, homologous adhesins or invasins immunoglobulin superfamily. This finding was confirmed using circular dichroism Fourier transform infrared spectrometric analysis domain Als1p. Specific amino acid hypervariability among proteins, energy-based models predicted similarities differences probably govern members. Collectively, results indicate structural functional diversity within provides array wall capable recognizing interacting during infection.