Heat shock protein SSA2 (SSA2)

Heat shock protein SSA2 is a member of the Hsp70 family of molecular chaperones, primarily characterized in the yeast Saccharomyces cerevisiae and the human pathogen Candida albicans. It functions as an ATP-dependent chaperone involved in essential cellular processes, including protein folding, the prevention of protein aggregation, and the translocation of polypeptides across membranes. In medical microbiology and pharmacology, SSA2 is recognized as a critical cell-surface receptor for Histatin 5, a human salivary antimicrobial peptide with potent fungicidal properties. The interaction between Histatin 5 and SSA2 is necessary for the peptide's internalization into the fungal cytoplasm, where it subsequently disrupts mitochondrial function and leads to cell death. Consequently, SSA2 is considered a significant target for the development of novel antifungal therapies, particularly for treating oral candidiasis. However, the high degree of structural conservation between fungal SSA2 and human Hsp70 homologs, such as HSPA8 (Hsc70), presents a challenge for achieving drug selectivity and avoiding potential host toxicity.

Other names

SSA2pStress-seventy subfamily A 2Hsp70 SSA2Ssa2

Binding to the chaperone on the cell surface to facilitate the intracellular translocation of antimicrobial peptides.