A product of RpfB and RipA joint enzymatic action promotes the resuscitation of dormant mycobacteria

Resuscitation promoting factor proteins (Rpfs) are known to participate in reactivating the dormant forms of actinobacteria. Structural analysis of the Rpf catalytic domain demonstrates its similarity to lysozyme and to lytic transglycosylases - the groups of enzymes that cleave the beta-1,4-glycosydic bond between N-acetylmuramic acid (N-AcMur) and N-acetylglucosamine (N-AcGlc) and concomitantly form a 1,6-anhydro ring at the N-AcMur residue. Analysis of the products formed from mycobacterial peptidoglycan hydrolysis reactions containing a mixture of RpfB and resuscitation promoting factor interacting protein (RipA) allowed us to identify the suggested product of their action - N-acetylglucosaminyl-beta(1-->4)-N-glycolyl-1,6-anhydromuramyl-L-alanyl-D-isoglut amate. To identify the role of this resulting product in resuscitation, we used a synthetic 1,6-anhydro disaccharide dipeptide and tested its ability to stimulate resuscitation using the dormant M. smegmatis model. It has been found that the disaccharide-dipeptide is the minimal structure capable of resuscitating the dormant mycobacterial cells over the concentration range of 9 - 100 ng/ml. The current study provides, therefore, the first insight into the molecular mechanism of resuscitation from dormancy involving a product of RpfB/RipA-mediated peptidoglycan cleavage. This article is protected by copyright. All rights reserved.

A product of RpfB and RipA joint enzymatic action promotes the resuscitation of dormant mycobacteria

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