Resuscitation-promoting factor B (RpfB)

Resuscitation-promoting factor B (RpfB) is a secreted muralytic enzyme produced by Mycobacterium tuberculosis that is essential for the reactivation of the pathogen from a dormant or latent state [1, 2]. It functions by hydrolyzing the peptidoglycan layer of the bacterial cell wall, a process that triggers metabolic activity and growth in quiescent bacilli [3, 9]. Structurally, RpfB is the most complex of the five Rpf homologs found in M. tuberculosis (RpfA-E), featuring multiple binding domains including three DUF348 domains and a G5 domain that coordinate its enzymatic activity with other cell wall proteins like RipA [4, 11, 16]. This enzyme is considered a high-confidence drug target because latent tuberculosis affects approximately one-quarter of the global population and represents a massive reservoir for active disease [2, 6, 8]. Targeting RpfB with inhibitors, such as 2-nitrophenylthiocyanates (e.g., NPT7), aims to prevent the transition from latency to active infection, thereby potentially shortening treatment durations and reducing relapses [5, 7]. In addition to its role in resuscitation, RpfB is a known immunogen that can elicit host antibody responses, making it a subject of interest for both diagnostic biomarkers and vaccine development [13, 15].

Other names

RpfBRv1009Resuscitation-promoting factor RpfBPeptidoglycan hydrolase RpfBMuralytic enzyme RpfB

Inhibition of muralytic enzymatic activity to prevent bacterial resuscitation from dormancy.