Sensitivity of to the bacteriocin mesentericin Y105 was previously shown to be dependent on the σ subunit of the RNA polymerase. This points towards expression of particular σ-dependent genes. The present study describes first, ManR, a new σ-associated activator, and second, \(EII_{t}^{Man}\) , a new σ-dependent PTS permease of the mannose family, both involved in sensitivity to mesentericin Y105, since interruption of their corresponding genes led to resistance of EGDe. \(EII_{t}^{Man}\) is likely composed of three subunits encoded by the operon (, and genes). Interruption of either the proximal () or distal () gene led to resistance, supporting results obtained in . Accordingly, such PTS permeases of the mannose family should be involved in sensitivity of different target strains to mesentericin Y105. In , expression of the operon is shown to be controlled by σ and ManR and to be induced by both glucose and mannose. The latter result indicates that these sugars are transported by the \(EII_{t}^{Man}\) permease. Moreover, these sugars correlatively induce sensitivity of to mesentericin Y105, strongly favouring the primary role of \(EII_{t}^{Man}\) . MptD, a membrane subunit of \(EII_{t}^{Man}\) , presents an additional domain compared to most IID subunits described in data banks. An in-frame deletion of this domain in led to resistance of , showing its connection with sensitivity and suggesting that it could be directly involved in the recognition of the target cell by mesentericin Y105. Taken together, the results of this work demonstrate that \(EII_{t}^{Man}\) is prominent in sensitivity to mesentericin Y105 and could be a receptor for subclass IIa bacteriocins.


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