Klebsiella pneumoniae carbapenemase 3 (KPC-3)

Klebsiella pneumoniae carbapenemase 3 (KPC-3) is a plasmid-encoded Class A serine beta-lactamase that confers high-level resistance to a broad spectrum of beta-lactam antibiotics, including penicillins, cephalosporins, and carbapenems [4, 5, 9]. It is one of the most prevalent carbapenemases globally, particularly within the Enterobacteriaceae family, and is a major driver of multidrug-resistant (MDR) hospital-acquired infections such as pneumonia, urinary tract infections, and bloodstream infections [3, 6, 14]. KPC-3 functions by utilizing an active-site serine residue to hydrolyze the beta-lactam ring, thereby inactivating the antibiotic before it can reach its bacterial target [5, 12]. Due to its clinical significance, KPC-3 is a primary target for novel beta-lactamase inhibitors such as avibactam, vaborbactam, and relebactam, which are administered in combination with beta-lactams to restore their efficacy [1, 2, 6]. However, the emergence of KPC-3 variants and mutations that confer resistance to these newer inhibitor combinations poses a significant challenge to modern antimicrobial therapy [3, 13].

Other names

blaKPC-3KPC-3 beta-lactamaseClass A carbapenemaseSerine carbapenemaseGroup 2f carbapenemase

Beta-lactamase inhibition