Literature DB >> 20674740

The polypeptide core of Microcin E492 stably associates with the mannose permease and interferes with mannose metabolism.

Sylvain Biéler1, Filo Silva, Dominique Belin.   

Abstract

Microcin E492 (MccE492) is an antibacterial protein whose activity on target cells requires ManYZ, the inner membrane component of the mannose permease. We show here that MceA, the polypeptide core of MccE492, stably associates with ManYZ both in the presence and in the absence of MceB, the MccE492 immunity protein. The two known physiological activities of the mannose permease were assayed in cells co-expressing MceA and MceB. Under these conditions, growth on mannose as the sole carbon source is prevented; this was not observed in cells expressing only MceB. In contrast, susceptibility to bacteriophage λ infection was not affected.
Copyright © 2010 Elsevier Masson SAS. All rights reserved.

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Year:  2010        PMID: 20674740     DOI: 10.1016/j.resmic.2010.07.003

Source DB:  PubMed          Journal:  Res Microbiol        ISSN: 0923-2508            Impact factor:   3.992


  5 in total

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Authors:  Guangshun Wang
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Review 4.  Bacteriocins, Antimicrobial Peptides from Bacterial Origin: Overview of Their Biology and Their Impact against Multidrug-Resistant Bacteria.

Authors:  Alexis Simons; Kamel Alhanout; Raphaël E Duval
Journal:  Microorganisms       Date:  2020-04-27

5.  The bacteriocin Angicin interferes with bacterial membrane integrity through interaction with the mannose phosphotransferase system.

Authors:  Verena Vogel; Lia-Raluca Olari; Marie Jachmann; Sebastian J Reich; Michelle Häring; Ann-Kathrin Kissmann; Frank Rosenau; Christian U Riedel; Jan Münch; Barbara Spellerberg
Journal:  Front Microbiol       Date:  2022-09-06       Impact factor: 6.064

  5 in total

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