Molecular Chaperone ClpB Becomes a Novel Antimicrobial Target

Abstract

Proteins are the most versatile and complicated biological macromolecules. Protein aggregation is defined as a non-physiological association of misfolded/partially folded polypeptides. Proteostasis prevents or minimizes protein aggregation and keeps proteins soluble and active. In live cells, molecular chaperones and their regulators facilitate protein quality control and proteostasis. A molecular chaperone is a protein that helps other proteins reach their physiologically active native conformation without being present in the client protein's final functional structure. These proteins help de novo protein folding and refolding of misfolded/partially folded proteins under cellular stresses and thereby inhibit protein aggregation.